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List of all mutants in PLPMDB (click to Mutant accession number to have all data about the mutant)

Title of reference

1  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Gly 170 Arg ; Ile 340 Met ; Pro 11 Leu ;
2  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Gly 82 Glu ;
3  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Pro 11 Leu ; Gly 170 Arg ; Ile 340 Met ;
4  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Pro 11 Leu ;
5  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Ile 340 Met ;
6  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Pro 11 Leu ; Ile 340 Met ;
7  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Gly 170 Arg ; Ile 340 Met ; Pro 11 Leu ;
8  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Gly 170 Arg ;
9  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Ile 244 Thr ;
10  Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.  Mutations: Lys 209 Arg ;
11  Reversible dissociation/association of D-amino acid transaminase subunits. Properties of isolated active dimers and inactive monomers.  Mutations: Trp 139 Phe ;
16  Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D- and L-alanine  Mutations: His 228 Asn ;
17  The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5'-phosphate produced by substitution of aspartic acid for glycine.  Mutations: Gly 279 Asp ;
18  The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5'-phosphate produced by substitution of aspartic acid for glycine.  Mutations: Gly 281 Asp ;
22  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: His 86 Leu ;
23  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Lys 87 Thr ;
24  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Arg 148 Gly ;
25  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Cys 170 Ser ;
26  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Cys 230 Ser ;
27  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Cys 230 Ala ;
28  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Cys 81 Ser ;
29  The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230.  Mutations: Cys 118 Ser ;
30  Evidence that cysteine 298 is in the active site of tryptophan indole-lyase.  Mutations: Cys 294 Ser ;
31  Evidence that cysteine 298 is in the active site of tryptophan indole-lyase.  Mutations: Cys 298 Ser ;
32  Contribution of a conserved arginine near the active site of Escherichia coli D-serine dehydratase to cofactor affinity and catalytic activity.  Mutations: Arg 120 Leu ;
33  Contribution of a conserved arginine near the active site of Escherichia coli D-serine dehydratase to cofactor affinity and catalytic activity.  Mutations: Ile 117 Leu ;
34  Contribution of a conserved arginine near the active site of Escherichia coli D-serine dehydratase to cofactor affinity and catalytic activity.  Mutations: Lys 118 His ;
35  The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.  Mutations: Tyr 214 Phe ;
36  Site-directed mutagenesis of the beta subunit of tryptophan synthase from Salmonella typhimurium. Role of active site glutamic acid 350.  Mutations: Glu 350 Gln ;
37  Site-directed mutagenesis of the beta subunit of tryptophan synthase from Salmonella typhimurium. Role of active site glutamic acid 350.  Mutations: Glu 350 Ala ;
38  Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine.  Mutations: Lys 145 Arg ;
39  Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine.  Mutations: Lys 145 Ala ;
40  Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.  Mutations: Asp 211 Ala ;
41  Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.  Mutations: Asp 211 Asn ;
42  Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.  Mutations: Asp 211 Glu ;
43  Heme biosynthesis in mammalian systems evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase.  Mutations: Lys 313 Ala ;
44  Heme biosynthesis in mammalian systems evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase.  Mutations: Lys 313 His ;
45  Lysine 258 in aspartate aminotransferase. Enforcer of the circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift.  Mutations: Lys 246 Ala ;
46  Lysine 258 in aspartate aminotransferase. Enforcer of the circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift.  Mutations: Lys 246 Met ;
47  Lysine 258 in aspartate aminotransferase. Enforcer of the circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift.  Mutations: Lys 246 Cys ;
48  Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy.  Mutations: Tyr 214 Phe ;
49  Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy.  Mutations: Lys 246 Ala ;
50  Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme  Mutations: Tyr 214 Arg ;
51  Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme  Mutations: Arg 374 Ala ;
52  Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme  Mutations: Tyr 214 Arg ;
53  Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme  Mutations: Arg 374 Ala ;
54  Site-directed mutagenesis of tyrosine-71 to phenylalanine in Citrobacter freundii tyrosine phenol-lyase: evidence for dual roles of tyrosine-71 as a general acid catalyst in the reaction mechanism and in cofactor binding.  Mutations: Tyr 71 Phe ;
56  Structure and function of the tryptophan synthase alpha(2)beta(2) complex. Roles of beta subunit histidine 86.  Mutations: His 86 Leu ;
57  Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.  Mutations: Arg 100 Thr ;
58  Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.  Mutations: Arg 100 Thr ;
59  Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.  Mutations: Val 283 Arg ;
60  Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.  Mutations: Val 283 Arg ;
61  Asp-89: a critical residue in maintaining the oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase  Mutations: Asp 89 Asn ;
62  Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps.  Mutations: Lys 69 Arg ;
63  Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps.  Mutations: Lys 69 Ala ;
64  Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study  Mutations: Asp 271 Ala ;
65  Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study  Mutations: Asp 271 Asn ;
66  Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study  Mutations: Asp 271 Glu ;
67  Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study  Mutations: Thr 246 Ala ;
68  Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study  Mutations: Cys 311 Ala ;
69  Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5'-phosphate. Chemical rescue studies of Lys39 --> Ala mutant.  Mutations: Lys 39 Ala ;
74  Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog.  Mutations: Asp 211 Ala ;
75  The identification of a lysine residue reactive to pyridoxal-5-phosphate in the glycerol dehydrogenase from the thermophile Bacillus stearothermophilus.  Mutations: Lys 97 His ;
76  Pyridoxal phosphate binding to wild type, W330F, and C298S mutants of Escherichia coli apotryptophanase: unraveling the cold inactivation.  Mutations: Trp 330 Phe ;
77  Pyridoxal phosphate binding to wild type, W330F, and C298S mutants of Escherichia coli apotryptophanase: unraveling the cold inactivation.  Mutations: Cys 298 Ser ;
78  Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.  Mutations: Glu 177 Lys ;
79  Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.  Mutations: Ser 180 Ala ;
80  Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.  Mutations: Tyr 31 Gln ;
81  Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.  Mutations: Lys 145 Gln ;
82  Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.  Mutations: Lys 145 Asn ;
83  Mutation of aspartate-233 to valine in mouse ornithine decarboxylase reduces enzyme activity.  Mutations: Asp 233 Val ;
84  Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.  Mutations: Leu 201 Ala ;
85  Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor.  Mutations: Asp 279 Ala ;
86  Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor.  Mutations: Asp 279 Glu ;
88  The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase.  Mutations: Tyr 121 Phe ;
89  The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase.  Mutations: Tyr 121 His ;
90  Role of Arg-277 in the binding of pyridoxal 5'-phosphate to Trypanosoma brucei ornithine decarboxylase.  Mutations: Arg 277 Ala ;
91  The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.  Mutations: Arg 381 Ala ;
92  The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.  Mutations: Arg 381 Ile ;
93  The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.  Mutations: Arg 381 Val ;
94  The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: His 134 Asn ;
95  The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: His 147 Asn ;
96  The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: His 150 Asn ;
97  Role of Arg-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group.  Mutations: Arg 401 Ala ;
98  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Ala--Lys 1-6 ;
99  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Ala--Trp 1-14 ;
100  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Ala--Val 1-30 ;
101  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Ala--Leu 1-49 ;
102  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Ala--Arg 1-58 ;
103  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Ala--Gly 1-75 ;
104  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Gln--Phe 435-483 ;
105  Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Leu--Phe 299-483 ;
106  Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.  Mutations: Lys 246 His ;
107  Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.  Mutations: Lys 250 His ;
108  Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine.  Mutations: Lys 246 gamma-thia-Lys ; Cys 389 Ala ; Cys 258 Ala ; Cys 77 Ala ; Cys 180 Ala ; Cys 181 Ala ;
109  Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysis.  Mutations: Lys 313 Gly ;
110  Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysis.  Mutations: Lys 313 His ;
111  Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysis.  Mutations: Lys 313 Arg ;
112  The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase.  Mutations: Arg 363 Ala ;
113  The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase.  Mutations: Arg 363 Lys ;
114  The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase.  Mutations: Arg 372 Ala ;
115  The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase.  Mutations: Arg 372 Lys ;
116  X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase.  Mutations: Thr 388 Ser ;
117  Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.  Mutations: Ala 143 Asp ; Ile 151 Phe ; Asn 150 Lys ; Gly 146 Lys ; Gly 147 Val ;
118  Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.  Mutations: Gly 144 Ala ;
119  Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.  Mutations: His 141 Tyr ; Ala 143 Val ; Ala 145 Thr ; Ile 151 Leu ;
120  Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.  Mutations: His 141 Leu ; Ala 145 Ser ; Gly 147 Ala ;
121  Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.  Mutations: Gly 142 Ala ; Ala 145 Ser ;
122  Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site.  Mutations: Ala 143 Val ; Gly 144 Gln ; Arg 149 Ser ; Ile 151 Leu ;
123  Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase.  Mutations: Lys 229 Gln ;
124  Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase.  Mutations: Lys 229 Arg ;
125  Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase.  Mutations: Lys 229 Arg ;
126  Mutant aspartate aminotransferase (K258H) without pyridoxal-5'-phosphate-binding lysine residue. Structural and catalytic properties.  Mutations: Lys 246 His ;
127  Mutant aspartate aminotransferase (K258H) without pyridoxal-5'-phosphate-binding lysine residue. Structural and catalytic properties.  Mutations: Lys 250 His ;
128  Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5'-phosphate.  Mutations: Lys 145 Asn ;
129  Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5'-phosphate.  Mutations: Lys 145 Gln ;
130  Studies of the active-site lysyl residue of thermostable aspartate aminotransferase: combination of site-directed mutagenesis and chemical modification.  Mutations: Lys 239 Cys ;
131  Studies of the active-site lysyl residue of thermostable aspartate aminotransferase: combination of site-directed mutagenesis and chemical modification.  Mutations: Lys 239 S-aminoethyl-Cys ;
132  Studies of the active-site lysyl residue of thermostable aspartate aminotransferase: combination of site-directed mutagenesis and chemical modification.  Mutations: Lys 239 S-aminopropyl-Cys ;
133  Studies of the active-site lysyl residue of thermostable aspartate aminotransferase: combination of site-directed mutagenesis and chemical modification.  Mutations: Lys 239 S-aminoethylthio-Cys ;
134  The role of Lys272 in the pyridoxal 5-phosphate active site of Synechococcus glutamate-1-semialdehyde aminotransferase.  Mutations: Lys 272 Arg ;
135  The role of Lys272 in the pyridoxal 5-phosphate active site of Synechococcus glutamate-1-semialdehyde aminotransferase.  Mutations: Lys 272 Ile ;
136  The role of Lys272 in the pyridoxal 5-phosphate active site of Synechococcus glutamate-1-semialdehyde aminotransferase.  Mutations: Lys 272 Glu ;
137  Serine hydroxymethyltransferase: origin of substrate specificity.  Mutations: Thr 224 Ala ;
138  Serine hydroxymethyltransferase: origin of substrate specificity.  Mutations: Thr 225 Ala ;
139  Serine hydroxymethyltransferase: origin of substrate specificity.  Mutations: Thr 226 Ala ;
140  Serine hydroxymethyltransferase: origin of substrate specificity.  Mutations: Thr 227 Ala ;
141  Serine hydroxymethyltransferase: origin of substrate specificity.  Mutations: Thr 230 Ala ;
142  Serine hydroxymethyltransferase: origin of substrate specificity.  Mutations: Thr 226 Ser ;
143  Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.  Mutations: Ala--Pro 1-3 ;
144  Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.  Mutations: Ala--Val 1-5 ;
145  Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.  Mutations: Ala--Phe 1-6 ;
146  Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.  Mutations: Ala--Ala 1-7 ;
147  Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.  Mutations: Ala--Val 1-9 ;
148  Structural and functional role of the amino-terminal region of porcine cytosolic aspartate aminotransferase. Catalytic and structural properties of enzyme derivatives truncated on the amino-terminal side.  Mutations: Ala--Pro 1-10 ;
149  Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.  Mutations: Glu 109 Ala ;
150  Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.  Mutations: Leu 188 Phe ;
151  Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.  Mutations: Asp 305 Asn ;
152  Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.  Mutations: Phe 306 Ala ;
153  Mechanism of mutual activation of the tryptophan synthase alpha and beta subunits. Analysis of the reaction specificity and substrate-induced inactivation of active site and tunnel mutants of the beta subunit.  Mutations: Glu 350 Ala ;
154  Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine.  Mutations: Tyr 265 Ala ;
155  Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine.  Mutations: Tyr 265 Ser ;
156  Tyrosine 265 of alanine racemase serves as a base abstracting alpha-hydrogen from L-alanine: the counterpart residue to lysine 39 specific to D-alanine.  Mutations: Tyr 265 Phe ;
157  A change in reaction specificity of sheep liver serine hydroxymethyltransferase. Induction of NADH oxidation upon mutation of His230 to Tyr.  Mutations: His 230 Tyr ;
158  A change in reaction specificity of sheep liver serine hydroxymethyltransferase. Induction of NADH oxidation upon mutation of His230 to Tyr.  Mutations: His 230 Ala ;
159  A change in reaction specificity of sheep liver serine hydroxymethyltransferase. Induction of NADH oxidation upon mutation of His230 to Tyr.  Mutations: His 230 Phe ;
160  A change in reaction specificity of sheep liver serine hydroxymethyltransferase. Induction of NADH oxidation upon mutation of His230 to Tyr.  Mutations: His 230 Asn ;
161  Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase. Schirch V.  Mutations: Tyr 65 Phe ;
162  Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase.Effects on catalytic properties.  Mutations: Asp 271 Glu ;
163  Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase.Effects on catalytic properties.  Mutations: His 192 Gln ;
164  Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase.Effects on catalytic properties.  Mutations: His 302 Gln ;
165  Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase.Effects on catalytic properties.  Mutations: Asn 300 Ala ;
166  The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase.  Mutations: Lys 256 Gln ;
167  The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase.  Mutations: Lys 256 Arg ;
168  The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.  Mutations: His 143 Ala ;
169  The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.  Mutations: His 143 Asn ;
170  Conversion of a PLP-Dependent Racemase into an Aldolase by a Single Active Site Mutation.  Mutations: Tyr 265 Ala ;
171  Identification of amino acid residues, essential for maintaining the tetrameric structure of sheep liver cytosolic serine hydroxymethyltransferase, by targeted mutagenesis.  Mutations: Trp 110 Ala ;
172  Identification of amino acid residues, essential for maintaining the tetrameric structure of sheep liver cytosolic serine hydroxymethyltransferase, by targeted mutagenesis.  Mutations: Trp 110 Phe ;
173  Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.  Mutations: Glu 49 Phe ;
174  Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.  Mutations: Gly 51 Leu ;
175  Evidence that mutations in a loop region of the alpha-subunit inhibit the transition from an open to a closed conformation in the tryptophan synthase bienzyme complex.  Mutations: Aps 60 Tyr ;
176  Disruption of active site interactions with pyridoxal 5'-phosphate and substrates by conservative replacements in the glycine-rich loop of Escherichia coli D-serine dehydratase.  Mutations: Cys 278 Ala ;
177  Disruption of active site interactions with pyridoxal 5'-phosphate and substrates by conservative replacements in the glycine-rich loop of Escherichia coli D-serine dehydratase.  Mutations: Gly 279 Ala ;
178  Disruption of active site interactions with pyridoxal 5'-phosphate and substrates by conservative replacements in the glycine-rich loop of Escherichia coli D-serine dehydratase.  Mutations: Gly 281 Ala ;
179  Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry.  Mutations: Ser 377 Asp ;
180  Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry.  Mutations: Ser 377 Glu ;
181  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 92 Leu ;
182  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 92 Trp ;
183  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Lys 278 Ala ;
184  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 92 Phe ;
185  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 92 Leu ; Lys 278 Ala ;
186  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 98 Gln ;
187  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 98 Glu ;
188  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Tyr 98 Gln ; Lys 282 Ala ;
189  Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites.  Mutations: Lys 282 Ala ; Tyr 98 Gln ;
190  The Contribution of a Conformationally Mobile, Active Site Loop to the Reaction Catalyzed by Glutamate Semialdehyde Aminomutase  Mutations: 159-172 Gly ;
191  Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants.  Mutations: Cys 360 Ala ;
192  Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants.  Mutations: Lys 69 Ala ;
193  Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase.  Mutations: Lys 258 Arg ;
194  Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis.  Mutations: His 228 Asn ;
195  Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.  Mutations: Lys 273 Ala ;
196  Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.  Mutations: Arg 407 Lys ;
197  Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.  Mutations: Tyr 233 Phe ;
198  Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli.  Mutations: Trp 248 Phe ;
199  Aspartate aminotransferase with the pyridoxal-5'-phosphate-binding lysine residue replaced by histidine retains partial catalytic competence.  Mutations: Lys 258 His ;
200  Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1.  Mutations: Leu 201 Trp ;
201  Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1.  Mutations: Leu 201 Ala ;
202  Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation.  Mutations: Ser 377 Ala ;
203  Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation.  Mutations: Ser 377 Asp ;
204  Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation.  Mutations: Ser 377 Glu ;
205  Lysine 87 in the beta subunit of tryptophan synthase that forms an internal aldimine with pyridoxal phosphate serves critical roles in transimination,catalysis, and product release.  Mutations: Lys 87 Thr ;
206  Determination of a functional lysine residue of a plant cysteine synthase bysite-directed mutagenesis, and the molecular evolutionary implications.  Mutations: Lys 49 Gly ;
207  Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase.  Mutations: Tyr 332 Phe ;
208  Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation.  Mutations: Cys 111 Ala ;
209  The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Glu 74 Lys ;
210  The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Glu 74 Gln ;
211  The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase.  Mutations: Tyr 82 Phe ;
212  Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding.  Mutations: Lys 396 Arg ;
213  Escherichia coli serine hydroxymethyltransferase. The role of histidine 228 in determining reaction specificity.  Mutations: His 228 Asn ;
214  Escherichia coli serine hydroxymethyltransferase. The role of histidine 228 in determining reaction specificity.  Mutations: His 228 Asp ;
215  Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.  Mutations: Tyr 225 Phe ;
216  Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.  Mutations: Tyr 225 Arg ;
217  Replacement of active-site lysine-239 of thermostable aspartate aminotransferase by S-(2-aminoethyl)cysteine: properties of the mutant enzyme.  Mutations: Lys 239 S-(2-aminoethyl)cysteine (SAEC) ;
218  Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase.  Mutations: His 65 Arg ;
219  Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase.  Mutations: Cys 52 Ala ;
220  Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase.  Mutations: Cys 52 Ser ;
221  Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli.  Mutations: Lys 276 His ;
222  Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli.  Mutations: Lys 276 Ala ;
223  The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.  Mutations: Cys 191 Phe ;
224  The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.  Mutations: Cys 191 Ser ;
225  The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.  Mutations: Cys 191 Trp ;
226  His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis.  Mutations: His 230 Arg ;
227  His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis.  Mutations: His 230 Phe ;
228  His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis.  Mutations: His 230 Tyr ;
229  The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation.  Mutations: Arg 391 Ala ;
230  Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity.  Mutations: Asp 305 Ala ;
231  The molecular pathway for the allosteric regulation of tryptophan synthase.  Mutations: Ser 178 Pro ;
232  Structure-function relationship in serine hydroxymethyltransferase.  Mutations: Glu 74 Gln ;
233  Structure-function relationship in serine hydroxymethyltransferase.  Mutations: Glu 74 Lys ;
234  Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors.  Mutations: Lys 69 Ala ;
235  Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors.  Mutations: Cys 70 Ala ;
236  Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors.  Mutations: Cys 360 Ala ;
237  The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate.  Mutations: Lys 258 Arg ;
238  Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding.  Mutations: Ser 180 Ala ;
239  Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding.  Mutations: Tyr 31 Gln ;
240  Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase.  Mutations: Cys 142 Gly ;
241  Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase.  Mutations: Cys 164 Gly ;
242  Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase.  Mutations: Cys 212 Gly ;
243  Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase.  Mutations: Ser 146 Ala ;
244  Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction.  Mutations: Ser 272 Ala ;
245  L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis.  Mutations: Lys 224 Ala ;
246  L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis.  Mutations: Lys 51 Ala ;
247  L-allo-threonine aldolase from Aeromonas jandaei DK-39: gene cloning, nucleotide sequencing, and identification of the pyridoxal 5'-phosphate-binding lysine residue by site-directed mutagenesis.  Mutations: Lys 199 Ala ;
248  The mechanism of high-yielding chiral syntheses catalysed by wild-type and mutant forms of aspartate aminotransferase.  Mutations: Arg 292 Asp ;
249  Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase. Effects of exogenous amines on the slow formation of intermediates.  Mutations: Lys 145 Gln ;
250  Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis.  Mutations: Gly 144 Ala ;
251  Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis.  Mutations: Gly 144 Ser ;
252  Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis.  Mutations: Gly 144 Thr ;
253  Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis.  Mutations: Gly 142 Cys ;
254  Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change.  Mutations: Asp 222 Ala ;
255  Alpha,beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required?  Mutations: Ser 272 Asp ;
256  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 214 Gly ;
257  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 214 Ala ;
258  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 218 Gly ;
259  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 218 Ala ;
260  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 258 Ala ;
261  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 258 Gly ;
262  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 264 Gly ;
263  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 264 Ala ;
264  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 216 Gly ;
265  Role of proline residues in the folding of serine hydroxymethyltransferase.  Mutations: Pro 216 Ala ;
266  Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction.  Mutations: Lys 51 Thr ;
267  Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction.  Mutations: Tyr 295 Phe ;
268  Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.  Mutations: Tyr 70 Ser ;
269  Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.  Mutations: Tyr 70 Phe ;
270  Bacterial selenocysteine synthase--structural and functional properties.  Mutations: Lys 295 Asn ;
271  Bacterial selenocysteine synthase--structural and functional properties.  Mutations: Lys 224 Asn ;
272  Bacterial selenocysteine synthase--structural and functional properties.  Mutations: Lys 328 Asn ;
273  Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.  Mutations: Cys 100 Ala ;
274  Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.  Mutations: Cys 176 Ala ;
275  Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.  Mutations: Cys 323 Ala ;
276  Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.  Mutations: Cys 358 Ala ;
277  Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.  Mutations: Cys 364 Ala ;
278  Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R.  Mutations: Lys 265 Arg ;
279  Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.  Mutations: Cys 328 Ala ;
280  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Gly 45 Thr ; Val 46 Pro ; Ala 44 Val ;
281  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Ala 52 Cys ;
282  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Pro 54 Asp ;
283  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Gly 319 Trp ;
284  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Ser 322 Ala ;
285  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Ser 322 Thr ;
286  Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes.  Mutations: Gly 350 Asp ;
287  Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558.  Mutations: Lys 207 Ala ;
288  Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558.  Mutations: Lys 207 Arg ;
289  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Ala ;
290  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Cys ;
291  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Asp ;
292  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Glu ;
293  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Phe ;
294  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 His ;
295  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Ile ;
296  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Lys ;
297  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Leo ;
298  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Met ;
299  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Asn ;
300  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Pro ;
301  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Gln ;
302  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Arg ;
303  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Ser ;
304  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Thr ;
305  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Val ;
306  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Trp ;
307  Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers.  Mutations: Gly 387 Tyr ;
308  Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase.  Mutations: Lys 39 Ala ;
309  Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase.  Mutations: His 166 Ala ;
310  Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase.  Mutations: Asp 444 Asn ;
311  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Pro--Ala 1-70 ; Asp--Lys 401-551 ;
312  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Pro--Ala 1-70 ;
313  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Pro--Glu 1-39 ;
314  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Ala--Lys 544-551 ;
315  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Val--Lys 534-551 ;
316  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Phe--Lys 442-551 ;
317  Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation.  Mutations: Gln--Lys 414-551 ;
318  Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.  Mutations: Val 39 Phe ;
319  Role of aspartate-133 and histidine-458 in the mechanism of tryptophan indole-lyase from Proteus vulgaris.  Mutations: Asp 133 Ala ;
320  Role of aspartate-133 and histidine-458 in the mechanism of tryptophan indole-lyase from Proteus vulgaris.  Mutations: His 458 Ala ;
321  Ornithine decarboxylase promotes catalysis by binding the carboxylate in a buried pocket containing phenylalanine 397.  Mutations: Phe 397 Ala ;
322  Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.  Mutations: Thr 124 Ala ;
323  Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.  Mutations: Thr 124 Asp ;
324  Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine.  Mutations: Phe 448 His ;
325  Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.  Mutations: Ile 232 Ala ; Tyr 233 Phe ;
326  Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.  Mutations: Ile 232 Ala ;
327  Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.  Mutations: Asp 230 Glu ;
328  Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.  Mutations: Glu 47 Asp ;
329  Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.  Mutations: Glu 47 Gln ;
330  Role of tyrosine 114 of L-methionine gamma-lyase from Pseudomonas putida.  Mutations: Tyr 114 Phe ;
331  Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.  Mutations: Asn 194 Ala ;
332  Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.  Mutations: Arg 386 Ala ;
333  Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.  Mutations: Arg 292 Ala ;
334  Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.  Mutations: Ser 311 Gly ; Ser 361 Phe ; Ile 353 Thr ; Phe 24 Leu ; Ala 11 Thr ; Ser 139 Gly ; Met 397 Leu ; Ser 363 Gly ; Val 387 Leu ; Ala 293 Val ; Asn 142 Thr ; Lys 126 Arg ; Lys 41 Asn ; Ile 37 Met ; Asn 34 Asp ; Ala 269 Thr ; Asn 297 Ser ;
335  Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate.  Mutations: Cys 42 Ser ;
336  Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate.  Mutations: Cys 42 Ala ;
337  Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.  Mutations: Arg 292 Lys ;
338  Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.  Mutations: Arg 386 Lys ;
339  Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.  Mutations: Arg 292 Lys ; Arg 386 Lys ;
340  An anomalous side reaction of the Lys303 mutant aromatic L-amino acid decarboxylase unravels the role of the residue in catalysis.  Mutations: Lys 303 Ala ;
341  Substitutions of alanine for cysteine at a reactive thiol site and for lysine at a pyridoxal phosphate binding site of 1-aminocyclopropane-1-carboxylate deaminase.  Mutations: Cys 162 Ala ;
342  Substitutions of alanine for cysteine at a reactive thiol site and for lysine at a pyridoxal phosphate binding site of 1-aminocyclopropane-1-carboxylate deaminase.  Mutations: Cys 162 Val ;
343  Substitutions of alanine for cysteine at a reactive thiol site and for lysine at a pyridoxal phosphate binding site of 1-aminocyclopropane-1-carboxylate deaminase.  Mutations: Cys 162 Gly ;
344  Substitutions of alanine for cysteine at a reactive thiol site and for lysine at a pyridoxal phosphate binding site of 1-aminocyclopropane-1-carboxylate deaminase.  Mutations: Lys 51 Ala ;
345  Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1.  Mutations: Tyr 31 Ala ;
346  Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1.  Mutations: Glu 32 Ala ;
347  Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1.  Mutations: Val 33 Ala ;
348  Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1.  Mutations: Lys 35 Ala ;
349  Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer.  Mutations: Trp 16 Phe ;
350  Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer.  Mutations: Trp 183 Phe ;
351  Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer.  Mutations: Trp 385 Phe ;
352  A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst.  Mutations: Lys 42 Ala ;
353  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: His 192 Ala ;
354  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Asp 252 Ala ;
355  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Asp 271 Ala ;
356  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Ser 296 Ala ;
357  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Lys 303 Ala ;
358  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Tyr 332 Ala ;
359  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Arg 355 Ala ;
360  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Asp 252 Glu ;
361  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Lys 303 Arg ;
362  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Tyr 332 Phe ;
363  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Arg 355 Lys ;
364  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Thr 246 Ala ;
365  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: His 269 Ala ;
366  Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis.  Mutations: Trp 363 Leu ;
367  Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase.  Mutations: Lys 229 Gln ;
368  Interaction of pyridoxal 5'-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase.  Mutations: Trp 139 Phe ;
369  Interaction of pyridoxal 5'-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase.  Mutations: Trp 139 His ;
370  Interaction of pyridoxal 5'-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase.  Mutations: Trp 139 Pro ;
371  Interaction of pyridoxal 5'-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase.  Mutations: Trp 139 Ala ;
372  Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.  Mutations: Lys 258 gamma-thiahomolysine ;
373  Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.  Mutations: Lys 258 gamma-dithiohomolysine ;
374  Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.  Mutations: Lys 258 carboxymethylcysteine ;
375  Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.  Mutations: Lys 258 carboxyethylcysteine ;
376  beta-Cystathionase from Bordetella avium. Role(s) of lysine 214 and cysteine residues in activity and cytotoxicity.  Mutations: Lys 214 Ala ;
377  beta-Cystathionase from Bordetella avium. Role(s) of lysine 214 and cysteine residues in activity and cytotoxicity.  Mutations: Cys 88 Ala ;
378  beta-Cystathionase from Bordetella avium. Role(s) of lysine 214 and cysteine residues in activity and cytotoxicity.  Mutations: Cys 279 Gly ;
379  beta-Cystathionase from Bordetella avium. Role(s) of lysine 214 and cysteine residues in activity and cytotoxicity.  Mutations: Cys 117 Gly ;
381  Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes.  Mutations: Phe 280 Cys ;
382  Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes.  Mutations: Phe 280 Ser ;
383  Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes.  Mutations: Cys 170 Phe ;
384  Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes.  Mutations: Cys 170 Trp ;
385  Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes.  Mutations: Cys 170 N-ethylmaleimide ;
386  Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes.  Mutations: Cys 170 methyl methanethiolsulfonate ;
387  NMR studies of 1H resonances in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli.  Mutations: His 143 Ala ;
388  NMR studies of 1H resonances in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli.  Mutations: His 143 Asp ;
389  NMR studies of 1H resonances in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli.  Mutations: Trp 140 Phe ;
390  NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase.  Mutations: His 68 Lys ;
391  NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase.  Mutations: His 143 Gln ;
392  NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase.  Mutations: His 189 Gln ;
393  NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase.  Mutations: His 193 Gln ;
394  Threonine dehydratases of Corynebacterium glutamicum with altered allosteric control: their generation and biochemical and structural analysis.  Mutations: Val 323 Ala ;
395  Threonine dehydratases of Corynebacterium glutamicum with altered allosteric control: their generation and biochemical and structural analysis.  Mutations: His 278 Arg ; Leu 351 Ser ;
396  Shift in pH-rate profile and enhanced discrimination between dicarboxylic and aromatic substrates in mitochondrial aspartate aminotransferase Y70H.  Mutations: Tyr 70 His ;
397  Role reversal for substrates and inhibitors. Slow inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors.  Mutations: Lys 145 Gln ;
398  Role reversal for substrates and inhibitors. Slow inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors.  Mutations: Lys 145 Asn ;
399  A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase.  Mutations: Asn 194 Ala ;
400  A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase.  Mutations: Asn 194 Ala ; Tyr 225 Phe ;
401  Dominant negative mutants of ornithine decarboxylase.  Mutations: Lys 69 Arg ;
402  Dominant negative mutants of ornithine decarboxylase.  Mutations: Lys 115 Arg ;
403  Dominant negative mutants of ornithine decarboxylase.  Mutations: Lys 169 Arg ;
404  Substitution of glutamic acid 109 by aspartic acid alters the substrate specificity and catalytic activity of the beta-subunit in the tryptophan synthase bienzyme complex from Salmonella typhimurium.  Mutations: Glu 109 Asp ;
405  Autonomous folding and coenzyme binding of the excised pyridoxal 5'-phosphate binding domain of aspartate aminotransferase from Escherichia coli.  Mutations: Thr--Leu 47-329 ;
406  The environments of Trp-248 and Trp-330 in tryptophan indole-lyase from Escherichia coli.  Mutations: Trp 248 Phe ;
407  The environments of Trp-248 and Trp-330 in tryptophan indole-lyase from Escherichia coli.  Mutations: Trp 330 Phe ;
408  Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product.  Mutations: Cys 325 Ala ;
409  Role of arginine 439 in substrate binding of 5-aminolevulinate synthase.  Mutations: Arg 439 Lys ;
410  Role of arginine 439 in substrate binding of 5-aminolevulinate synthase.  Mutations: Arg 439 Leu ;
411  Role of arginine 439 in substrate binding of 5-aminolevulinate synthase.  Mutations: Arg 433 Lys ;
412  Role of arginine 439 in substrate binding of 5-aminolevulinate synthase.  Mutations: Arg 433 Leu ;
413  Directed evolution of an aspartate aminotransferase with new substrate specificities.  Mutations: Ala 269 Thr ; Val 387 Leu ; Met 397 Leu ; Ser 311 Gly ; Asn 297 Ser ; Ala 293 Val ; Ser 139 Gly ; Lys 126 Arg ; Lys 41 Asn ; Ala 11 Thr ; Ile 37 Met ; Asn 34 Asp ; Asn 142 Thr ;
414  Deletion of the regulatory domain in the pyridoxal phosphate-dependent heme protein cystathionine beta-synthase alleviates the defect observed in a catalytic site mutant.  Mutations: Val 168 Met ; Trp--Lys 409-550 ;
415  Deletion of the regulatory domain in the pyridoxal phosphate-dependent heme protein cystathionine beta-synthase alleviates the defect observed in a catalytic site mutant.  Mutations: Val 168 Met ;
416  Deletion of the regulatory domain in the pyridoxal phosphate-dependent heme protein cystathionine beta-synthase alleviates the defect observed in a catalytic site mutant.  Mutations: Trp--Lys 409-550 ;
417  The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-carboxylate synthase. Coenzyme binding, substrate binding, and beyond.  Mutations: Arg 286 Leu ;
418  Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate.  Mutations: Asn 185 Ala ;
419  Altering the reaction specificity of eukaryotic ornithine decarboxylase.  Mutations: Cys 360 Ala ;
420  Altering the reaction specificity of eukaryotic ornithine decarboxylase.  Mutations: Cys 360 Ser ;
421  Conformational changes and subunit communication in tryptophan synthase: effect of substrates and substrate analogs.  Mutations: Ala 129 Trp ;
422  The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.  Mutations: Asp 200 Asn ;
423  The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.  Mutations: Asp 200 Glu ;
424  The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.  Mutations: Asp 200 Ala ;
425  The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.  Mutations: Arg 235 Asp ;
426  The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.  Mutations: Arg 235 Gln ;
427  The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.  Mutations: Cys 191 Tyr ;
428  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Ala 221 Val ;
429  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Thr 83 Ala ;
430  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Thr 83 Ile ;
431  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Ala 84 Thr ;
432  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Ala 84 Val ;
433  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Cys 181 Arg ;
434  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Cys 181 Thr ;
435  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Glu 185 Gly ;
436  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Ala 188 Thr ;
437  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Asp 189 Gly ;
438  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Ile 215 Thr ;
439  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Ser 218 Arg ;
440  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Asn 219 Asp ;
441  X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression.  Mutations: Cys 181 Thr ; Thr 244 Tyr ;
442  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Ser 229 Ala ;
443  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Ser 229 Cys ;
444  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: His 231 Arg ;
445  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: His 231 Phe ;
446  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: His 231 Gln ;
447  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: His 231 Asn ;
448  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Lys 232 Ala ;
449  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Met 233 Ile ;
450  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Cys 240 Ala ;
451  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Cys 240 Ser ;
452  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Ser 322 Ala ;
453  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Ser 322 Thr ;
454  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Cys 329 Ala ;
455  Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues.  Mutations: Cys 329 Ser ;
456  Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.  Mutations: Asp 60 Asn ;
457  Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.  Mutations: Asp 60 Glu ;
458  Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.  Mutations: Asp 60 Ala ;
459  Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.  Mutations: Asp 60 Tyr ;
460  Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana.  Mutations: Cys 8 Ser ;
461  Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana.  Mutations: Ala 55 Gly ;
462  Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana.  Mutations: Ala 91 Gly ;
463  Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana.  Mutations: Thr 412 Pro ;
464  Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana.  Mutations: Gly 459 Ala ;
465  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ile 4 Leu ;
466  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Lys 17 Arg ;
467  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Met 106 Val ;
468  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Asp 126 Glu ;
469  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Glu 134 Ala ;
470  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ile 139 Val ;
471  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ala 159 Ser ;
472  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Asp 165 Asn ;
473  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Leu 248 Pro ;
474  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ser 292 Thr ;
475  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Asp 310 Asn ;
476  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ser 316 Arg ;
477  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ile 366 Leu ;
478  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Ile 373 Leu ;
479  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Lys 380 glu ;
480  The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403  Mutations: Thr 266 Asp ; Lys 268 Glu ;
481  The SPL1 tRNA splicing gene of Candida maltosa and Candida albicans.  Mutations: Glu 155 Ala ;
482  The SPL1 tRNA splicing gene of Candida maltosa and Candida albicans.  Mutations: Lys 217 ;
483  The SPL1 tRNA splicing gene of Candida maltosa and Candida albicans.  Mutations: Thr 374 Ala ;
484  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Asn 54 Lys ;
485  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Tyr 55 His ;
486  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Asn 89 Lys ;
487  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Gln 90 Glu ;
488  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Cys 93 Phe ;
489  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Arg 154 Leu ;
490  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Arg 180 Thr ;
491  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Ala 184 ;
492  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Ala 226 Val ;
493  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Pro 241 Leu ;
494  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Tyr 245 cys ;
495  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Arg 250 Pro ;
496  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Thr 267 Ile ;
497  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Ala 270 Pro ;
498  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Arg 271 lys ;
499  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: His 319 Tyr ;
500  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Val 332 Met ;
501  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Gly 353 Asp ;
502  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Gly 375 Ala ;
503  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Cys 394 Arg ;
504  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Leu 402 Pro ;
505  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Pro 417 Leu ;
506  Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene.  Mutations: Leu 437 Phe ;
507  Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs.  Mutations: Arg 39 Cys ;
508  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: tyr 199 His ;
509  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: Arg 294 Gln ;
510  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: Thr 388 Ser ;
511  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: Arg 411 Cys ;
512  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: Arg 448 Gln ;
513  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: Arg 452 Cys ;
514  Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.  Mutations: Ile 476 Asn ;
515  Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI.  Mutations: Val 222 Ile ;
516  Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI.  Mutations: Val 231 Glu ;
517  Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI.  Mutations: Asn 339 Ser ;
518  Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI.  Mutations: Asn 337 Lys ;
519  Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI.  Mutations: Arg 715 Ser ;
520  Cloning of bovine muscle glycogen phosphorylase cDNA and identification of a mutation in cattle with myophosphorylase deficiency, an animal model for McArdle's disease.  Mutations: Arg 489 Trp ;
521  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Leu 115 Pro ;
522  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Arg 193 Trp ;
523  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Gly 204 Ser ;
524  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Glu 348 Lys ;
525  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Thr 487 Asn ;
526  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Arg 601 Trp ;
527  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Ala 659 Asp ;
528  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Asn 684 Tyr ;
529  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Ala 703 Val ;
530  Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study.  Mutations: Trp 797 Arg ;
531  The molecular genetic basis of myophosphorylase deficiency (McArdle's disease).  Mutations: Leu 291 Pro ;
532  The molecular genetic basis of myophosphorylase deficiency (McArdle's disease).  Mutations: Leu 396 Pro ;
533  The molecular genetic basis of myophosphorylase deficiency (McArdle's disease).  Mutations: Lys 542 Thr ;
534  The molecular genetic basis of myophosphorylase deficiency (McArdle's disease).  Mutations: Glu 654 Lys ;
535  The molecular genetic basis of myophosphorylase deficiency (McArdle's disease).  Mutations: Phe 708 ;
536  Mutation analysis in myophosphorylase deficiency (McArdle's disease).  Mutations: Gln 665 Glu ;
537  Mutation analysis in myophosphorylase deficiency (McArdle's disease).  Mutations: Gly 685 Arg ;
538  Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease.  Mutations: Ala 686 Pro ;
539  Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.  Mutations: Arg 168 Cys ;
540  Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.  Mutations: Ala 192 Ser ;
541  Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.  Mutations: Ile 237 Leu ;
542  Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.  Mutations: Asp 240 Glu ;
543  Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.  Mutations: Gly 289 Asp ;
544  Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491.  Mutations: Thr 336 ser ;
545  Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.  Mutations: Pro 11 Leu ;
546  Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.  Mutations: Ile 340 Met ;
547  Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene.  Mutations: Ser 205 Pro ;
548  A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1.  Mutations: Gly 82 Glu ;
549  A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1.  Mutations: Ser 187 Phe ;
550  Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation.  Mutations: Gly 41 Arg ;
551  Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene.  Mutations: Arg 233 His ;
552  Gene symbol: AGXT. Disease: primary hyperoxaluria type I.  Mutations: Gly 41 Val ;
553  Gene symbol: AGXT. Disease: primary hyperoxaluria type I.  Mutations: Gly 116 Arg ;
554  Gene symbol: AGXT. Disease: primary hyperoxaluria type I.  Mutations: Gly 156 Arg ;
556  Identification of 5 novel mutations in the AGXT gene.  Mutations: Phe 152 ile ;
557  Identification of 5 novel mutations in the AGXT gene.  Mutations: Gly 170 Arg ;
558  Identification of 5 novel mutations in the AGXT gene.  Mutations: Asp 183 Asn ;
559  Identification of 5 novel mutations in the AGXT gene.  Mutations: Arg 233 Cys ;
560  Identification of 5 novel mutations in the AGXT gene.  Mutations: Ile 244 Thr ;
561  Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.  Mutations: Arg 499 Cys ;
562  Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.  Mutations: Arg 544 His ;
563  Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli.  Mutations: Asp 157 Asn ;
564  Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli.  Mutations: Phe 212 Tyr ;
565  Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli.  Mutations: Arg 397 Ser ;
566  Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli.  Mutations: Val 420 Ile ;
567  Lysine 238 is an essential residue for alpha,beta-elimination catalyzed by Treponema denticola cystalysin.  Mutations: Lys 238 Ala ;
568  Lysine 238 is an essential residue for alpha,beta-elimination catalyzed by Treponema denticola cystalysin.  Mutations: Lys 238 Arg ;
569  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Gln 26 Glu ;
570  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Gln 151 Ar ;
571  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Lys 178 Glu ;
572  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Glu 185 Asp ;
573  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Asn 191 Asp ;
574  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Glu 313 Asp ;
575  Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria.  Mutations: Asp 337 Asn ;
576  Genetic and biochemical characterization of the trpB8 mutation of Escherichia coli tryptophan synthase. An amino acid switch at the sharp turn of the trypsin-sensitive "hinge" region diminishes substrate binding and alters solubility.  Mutations: Gly 281 Arg ;
577  Anaerobiosis and plant growth hormones induce two genes encoding 1-aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.).  Mutations: Asn 129 Thr ;
578  Anaerobiosis and plant growth hormones induce two genes encoding 1-aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.).  Mutations: Phe 151 Leu ;
579  Anaerobiosis and plant growth hormones induce two genes encoding 1-aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.).  Mutations: Gly 273 Asp ;
580  Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II.  Mutations: Gly 362 Val ;
581  Molecular defect in a patient with pyridoxine-responsive homocystinuria.  Mutations: Ala 113 Val ;
582  Molecular defect in a patient with pyridoxine-responsive homocystinuria.  Mutations: Phe 144 Leu ;
583  Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system.  Mutations: Phe 77 Arg ;
584  Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system.  Mutations: Lys 101 Asn ;
585  Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria.  Mutations: Arg 124 Gln ;
586  Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria.  Mutations: Glu 130 Asp ;
587  A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype.  Mutations: Ile 277 Thr ;
588  A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype.  Mutations: Gly 138 Arg ;
589  A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype.  Mutations: Glu 143 Lys ;
590  The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations.  Mutations: Pro 87 Ser ;
591  The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations.  Mutations: Thr 256 Met ;
592  Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients.  Mutations: Cys 164 Tyr ;
593  Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients.  Mutations: Val 370 Met ;
594  A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene.  Mutations: Val 167 Met ;
595  A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene.  Mutations: Gly 306 Ser ;
596  A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene.  Mutations: Ala 330 Val ;
597  A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene.  Mutations: Val 453 Glu ;
598  Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient.  Mutations: Asp 443 Asn ;
599  Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations.  Mutations: Gly 115 Arg ;
600  Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations.  Mutations: Pro 289 Leu ;
601  Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria.  Mutations: Ala 330 Glu ;
602  Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria.  Mutations: Arg 438 Gln ;
603  Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria.  Mutations: Thr 352 Met ;
604  Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria.  Mutations: Thr 261 Met ;
605  Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria.  Mutations: Arg 265 Lys ;
606  Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria.  Mutations: Val 319 Ala ;
607  Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria.  Mutations: Arg 368 His ;
608  Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients.  Mutations: Lys 383 Glu ;
609  Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients.  Mutations: Lys 538 Ser ;
610  Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99.  Mutations: Glu 175 Lys ;
611  Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients.  Mutations: Cys 369 Tyr ;
612  Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients.  Mutations: Arg 438 Gln ;
613  Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype.  Mutations: Arg 57 Trp ;
614  Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype.  Mutations: Met 125 Val ;
615  Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype.  Mutations: Glu 301 Lys ;
616  Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype.  Mutations: Arg 335 Cys ;
617  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Pro 48 Leu ;
618  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Pro 77 Arg ;
619  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Gly 84 Arg ;
620  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Lys 101 Asn ;
621  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Lys 101 Gln ;
622  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 120 Cys ;
623  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 120 His ;
624  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 120 Leu ;
625  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 124 Trp ;
626  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Glu 127 Asp ;
627  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Gly 147 Arg ;
628  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Gly 150 Arg ;
629  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ala 158 ;
630  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ile 151 Met ;
631  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ala 154 Thr ;
632  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Val 179 Ala ;
633  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Thr 190 Met ;
634  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Asp 197 Val ;
635  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 223 His ;
636  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ala 225 Thr ;
637  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Asp 223 Asn ;
638  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Glu 238 Lys ;
639  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 265 Gly ;
640  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Glu 269 ;
641  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Gly 304 Arg ;
642  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 335 His ;
643  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ser 351 Asn ;
644  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Val 353 Met ;
645  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 368 Cys ;
646  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Lys 383 Asn ;
647  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Met 390 Ile ;
648  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Thr 433 Asn ;
649  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ile 434 Thr ;
650  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Ser 465 Leu ;
651  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Arg 490 Cys ;
652  Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells.  Mutations: Val 533 Asp ;
653  Pyridoxal phosphate-dependent histidine decarboxylases. Cloning, sequencing, and expression of genes from Klebsiella planticola and Enterobacter aerogenes and properties of the overexpressed enzymes.  Mutations: Ala 147 Thr ;
654  Pyridoxal phosphate-dependent histidine decarboxylases. Cloning, sequencing, and expression of genes from Klebsiella planticola and Enterobacter aerogenes and properties of the overexpressed enzymes.  Mutations: Gln 183 Glu ;
655  Characterization and expression of the complementary DNA encoding rat histidine decarboxylase.  Mutations: His 8 Arg ;
656  Characterization and expression of the complementary DNA encoding rat histidine decarboxylase.  Mutations: Val 28 Leu ;
657  Characterization and expression of the complementary DNA encoding rat histidine decarboxylase.  Mutations: Arg 286 Cys ;
658  A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid.  Mutations: Ala 92 Pro ;
659  A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid.  Mutations: Glu 124 Asp ;
660  A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid.  Mutations: Phe 261 Leu ;
661  A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid.  Mutations: Cys 375 Arg ;
662  A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid.  Mutations: Asp 380 Thr ; Asp 381 Thr ;
663  Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene.  Mutations: Val 474 Gly ;
664  Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene.  Mutations: Arg 532 Gln ;
665  Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene.  Mutations: Phe 565 Leu ;
666  Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis.  Mutations: Val 17 Met ;
667  Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis.  Mutations: Pro 210 Leu ;
668  Molecular cloning of genomic DNA and chromosomal assignment of the gene for human aromatic L-amino acid decarboxylase, the enzyme for catecholamine and serotonin biosynthesis.  Mutations: Met 217 Val ;
669  The molecular basis of glutamate formiminotransferase deficiency.  Mutations: Arg 135 Cys ;
670  The molecular basis of glutamate formiminotransferase deficiency.  Mutations: Arg 299 Pro ;
671  The molecular basis of glutamate formiminotransferase deficiency.  Mutations: Ala 438 Glu ;
672  4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency.  Mutations: Arg 220 Lys ;
673  Structural and expression analyses of normal and mutant mRNA encoding glycine decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia.  Mutations: Phe 756 ;
674  Identification of a common mutation in Finnish patients with nonketotic hyperglycinemia.  Mutations: Ser 564 Ile ;
675  Recurrent mutations in P- and T-proteins of the glycine cleavage complex and a novel T-protein mutation (N145I): a strategy for the molecular investigation of patients with nonketotic hyperglycinemia (NKH).  Mutations: Arg 515 Ser ;
676  Nonketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis.  Mutations: Ala 283 Pro ;
677  Nonketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis.  Mutations: Pro 329 Thr ;
678  The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, deletions, insertion elements and DNA islands.  Mutations: Arg 401 Cys ;
679  The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, deletions, insertion elements and DNA islands.  Mutations: Thr 416 Asn ;
680  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Gly 18 ser ;
681  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Glu 104 Asp ;
682  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Gly 221 Val ;
683  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Ser 227 Thr ;
684  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Glu 245 Lys ;
685  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Leu 270 Pro ;
686  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Glu 375 Asp ;
687  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Leu 411 Phe ;
688  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Ala 413 Val ;
689  A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene.  Mutations: Lys 466 Arg ;
690  Comparative genomes of Chlamydia pneumoniae and C. trachomatis.  Mutations: Lys 257 Gln ;
691  Characterization of histidinol phosphate aminotransferase from Escherichia coli.  Mutations: Lys 21 Ala ;
692  Characterization of histidinol phosphate aminotransferase from Escherichia coli.  Mutations: Asn 157 Ala ;
693  Characterization of histidinol phosphate aminotransferase from Escherichia coli.  Mutations: Arg 335 Leu ;
694  Characterization of histidinol phosphate aminotransferase from Escherichia coli.  Mutations: Asn 157 Ala ; Arg 335 Leu ;
695  Heterodimeric interactions among the 1-amino-cyclopropane-1-carboxylate synthase polypeptides encoded by the Arabidopsis gene family.  Mutations: Lys 278 Ala ;
696  Heterodimeric interactions among the 1-amino-cyclopropane-1-carboxylate synthase polypeptides encoded by the Arabidopsis gene family.  Mutations: Tyr 92 Ala ;
697  Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability.  Mutations: Trp 50 Tyr ;
698  Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability.  Mutations: Trp 161Tyr ;
699  On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.  Mutations: Thr 183 Val ;
700  Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.  Mutations: Tyr 17 Phe ;
701  Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.  Mutations: Tyr 144 Phe ;
702  Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.  Mutations: Asp 147 Asn ;
703  Three-dimensional structure of kynureninase from Pseudomonas fluorescens.  Mutations: Asp 132 ? ;
704  Three-dimensional structure of kynureninase from Pseudomonas fluorescens.  Mutations: Asp 201 ? ;
705  The critical structural role of a highly conserved histidine residue in group IIamino acid decarboxylases.  Mutations: His 241 ? ;
706  Serine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism.  Mutations: Glu 75 Gln ;
707  Serine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism.  Mutations: Glu 75 Leu ;
708  Substrate recognition mechanism of thermophilic dual-substrate enzyme.  Mutations: Ser 15 Asp ; Thr 17 Val ; Lys 109 Ser ; Ser 292 Arg ;
709  The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8.  Mutations: Lys 109 Val ;
710  The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8.  Mutations: Lys 109 Ser ;
711  Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.  Mutations: Pro 195 Ala ; Pro 138 Ala ;
712  Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.  Mutations: Pro 138 Ala ;
713  Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.  Mutations: Pro 195 Ala ;
714  Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis.  Mutations: Arg 253 Ala ;
715  Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.  Mutations: Ala 169 Leu ; Cys 170 Trp ;
716  Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.  Mutations: Asn 194 Ala ; Val 39 Phe ;
717  Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.  Mutations: Gly 121 Tyr ;
718  Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base.  Mutations: Lys 119 Ala ;
719  Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base.  Mutations: Pro--Ala 1-69 ;
720  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Arg 3963 Gln ;
721  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 3994 Glu ;
722  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 401 Glu ;
723  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 401 Gln ;
724  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 405 Glu ;
725  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 405 Gln ;
726  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: His 406 Asp ;
727  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: His 406 Asn ;
728  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Arg 407 Glu ;
729  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Arg 407 Gln ;
730  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Arg 412 Glu ;
731  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Arg 412 Gln ;
732  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 335 Gln ;
733  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: 244--249 ;
734  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 1341Gln ;
735  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 1342 Gln ;
736  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 346 Gln ;
737  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 354 Gln ;
738  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 3991 Glu ;
739  Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase.  Mutations: Lys 3991 Gln ;
740  Role of pro-297 in the catalytic mechanism of sheep liver serine hydroxymethyltransferase  Mutations: Pro 297 Arg ;
741  2H, 13C, and 15N kinetic isotope effects on the reaction of the ammonia-rescued K258A mutant of aspartate aminotransferase.  Mutations: Lys 258 Ala ;
742  The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.  Mutations: Arg 292 Asp ;
743  [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.  Mutations: Arg 292 Leu ;
744  [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids.  Mutations: Arg 292 Val ;
745  The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants.  Mutations: Glu 265 Gln ; Lys 68 Met ;
746  The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants.  Mutations: Lys 68 Glu ; Glu 265 Lys ;
747  Site-directed mutagenesis provides insight into racemization and transamination of alanine catalyzed by treponema denticola cystalysin.  Mutations: Lys 238 Ala ;
748  Site-directed mutagenesis provides insight into racemization and transamination of alanine catalyzed by treponema denticola cystalysin.  Mutations: Tyr 123 Phe ;
749  Site-directed mutagenesis provides insight into racemization and transamination of alanine catalyzed by treponema denticola cystalysin.  Mutations: Tyr 124 Phe ; Tyr 123 Phe ;
750  Site-directed mutagenesis of His343-->Ala in Citrobacter freundii tyrosine phenol-lyase. Effects on the kinetic mechanism and rate-determining step.  Mutations: His 343 Ala ;
751  Formation in vitro of hybrid dimers of H463F and Y74F mutant Escherichia coli tryptophan indole-lyase rescues activity with L-tryptophan.  Mutations: His 463 Phe ;
752  Formation in vitro of hybrid dimers of H463F and Y74F mutant Escherichia coli tryptophan indole-lyase rescues activity with L-tryptophan.  Mutations: Tyr 74 Phe ;
753  Structural Analysis of Pseudomonas 1-Aminocyclopropane-1-carboxylate Deaminase Complexes: Insight into the Mechanism of a Unique Pyridoxal-5'-phosphate Dependent Cyclopropane Ring-Opening Reaction(,).  Mutations: TYR 294 ? ;
754  Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.  Mutations: Trp 330 Phe ;
755  Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase.  Mutations: Tyr 74 Phe ;
756  Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.  Mutations: Arg 386 Phe ;

 

Query Results 741 mutants

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