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