all references in PLPMDB
| 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. || Comparative genomes of Chlamydia pneumoniae and C. trachomatis. || Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase. || Gene symbol: AGXT. Disease: primary hyperoxaluria type I. || 4-Aminobutyrate aminotransferase (GABA-transaminase) deficiency. || Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype. || The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, deletions, insertion elements and DNA islands. || Two Novel Mutations in the Cystathionine beta-synthase Gene of Homocystinuric Patients. || Asp-89: a critical residue in maintaining the oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase || 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. || Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps. || Deletion of the regulatory domain in the pyridoxal phosphate-dependent heme protein cystathionine beta-synthase alleviates the defect observed in a catalytic site mutant. || The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-carboxylate synthase. Coenzyme binding, substrate binding, and beyond. || Structure modelling and site-directed mutagenesis of the rat aromatic L-amino acid pyridoxal 5'-phosphate-dependent decarboxylase: a functional study || Structure and function of the tryptophan synthase alpha(2)beta(2) complex. Roles of beta subunit histidine 86. || Reversible dissociation/association of D-amino acid transaminase subunits. Properties of isolated active dimers and inactive monomers. || The Contribution of a Conformationally Mobile, Active Site Loop to the Reaction Catalyzed by Glutamate Semialdehyde Aminomutase || Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a. || A change in reaction specificity of sheep liver serine hydroxymethyltransferase.
Induction of NADH oxidation upon mutation of His230 to Tyr. || His230 of serine hydroxymethyltransferase facilitates the proton abstraction step in catalysis. || X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression. || The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. || Molecular cloning of the human and murine 2-amino-3-ketobutyrate coenzyme A ligase cDNAs. || Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. || Complete DNA sequence of a serogroup A strain of Neisseria meningitidis Z2491. || Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate. || Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase.
Schirch V. || Identification of 5 novel mutations in the AGXT gene. || Functional synergism between the most common polymorphism in
human alanine:glyoxylate aminotransferase and four of the
most common disease-causing mutations. || Role of pro-297 in the catalytic mechanism of sheep liver serine hydroxymethyltransferase || Altering the reaction specificity of eukaryotic ornithine decarboxylase. || The role of Glu74 and Tyr82 in the reaction catalyzed by sheep liver cytosolic serine hydroxymethyltransferase. || Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase. || Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes. || Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana. || Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. || Site-directed mutagenesis of K396R of the 65 kDa glutamic acid decarboxylase active site obliterates enzyme activity but not antibody binding. || Role of tyrosine 114 of L-methionine gamma-lyase from Pseudomonas putida. || 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). || A glutamate decarboxylase system protects Listeria monocytogenes in gastric fluid. || The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403 || Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase.Effects on catalytic properties. || Beta D305A mutant of tryptophan synthase shows strongly perturbed allosteric regulation and substrate specificity. || Substrate recognition mechanism of thermophilic dual-substrate enzyme. || Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant. || Nonketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis. || Molecular heterogeneity of myophosphorylase deficiency (McArdle's disease): a genotype-phenotype correlation study. || Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. || Formation in vitro of hybrid dimers of H463F and Y74F mutant Escherichia coli tryptophan indole-lyase rescues activity with L-tryptophan. || Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase. || Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with L-tyrosine. || The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants. || Two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease. || Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase. || Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase. || The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. || Deletion mutagenesis of human cystathionine beta-synthase. Impact on activity, oligomeric status, and S-adenosylmethionine regulation. || Contribution of Lys276 to the conformational flexibility of the active site of glutamate decarboxylase from Escherichia coli. || Identification of amino acid residues, essential for maintaining the tetrameric structure of sheep liver cytosolic serine hydroxymethyltransferase, by targeted mutagenesis. || Location of the pteroylpolyglutamate-binding site on rabbit cytosolic serine hydroxymethyltransferase. || On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase. || Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. || Characterization of the S272A,D site-directed mutations of O-acetylserine sulfhydrylase: involvement of the pyridine ring in the alpha,beta-elimination reaction. || Ornithine decarboxylase promotes catalysis by binding the carboxylate in a buried pocket containing phenylalanine 397. || Structure-function relationship in serine hydroxymethyltransferase. || Alpha,beta-elimination reaction of O-acetylserine sulfhydrylase. Is the pyridine ring required? || The molecular pathway for the allosteric regulation of tryptophan synthase. || Characterization of histidinol phosphate aminotransferase from Escherichia coli. || Role of proline residues in the folding of serine hydroxymethyltransferase. || Surface-exposed tryptophan residues are essential for O-acetylserine sulfhydrylase structure, function, and stability. || The molecular basis of glutamate formiminotransferase deficiency. || 2H, 13C, and 15N kinetic isotope effects on the reaction of the ammonia-rescued K258A mutant of aspartate aminotransferase. || Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction. || Lysine 238 is an essential residue for alpha,beta-elimination catalyzed by Treponema denticola cystalysin. || Conversion of a PLP-Dependent Racemase into an Aldolase by a Single Active Site Mutation. || A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. || 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. || 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. || A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. || Point mutations in the tyrosine aminotransferase gene in tyrosinemia type II. || Cloning and expression of the Erwinia herbicola tyrosine phenol-lyase gene in Escherichia coli. || Dominant negative mutants of ornithine decarboxylase. || Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5'-phosphate. || Role of aspartate-133 and histidine-458 in the mechanism of tryptophan indole-lyase from Proteus vulgaris. || The critical structural role of a highly conserved histidine residue in group IIamino acid decarboxylases. || Three-dimensional structure of kynureninase from Pseudomonas fluorescens. || Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis. || Heterodimeric interactions among the 1-amino-cyclopropane-1-carboxylate synthase polypeptides encoded by the Arabidopsis gene family. || Conformational changes and subunit communication in tryptophan synthase: effect of substrates and substrate analogs. || Pyridoxal 5'-phosphate dependent histidine decarboxylase. Overproduction, purification, biosynthesis of soluble site-directed mutant proteins, and replacement of conserved residues. || Serine Hydroxymethyltransferase: Role of Glu75 and Evidence that Serine Is Cleaved by a Retroaldol Mechanism. || Escherichia coli serine hydroxymethyltransferase. The role of histidine 228 in determining reaction specificity. || Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base. || Site-directed mutagenesis provides insight into racemization and transamination of alanine catalyzed by treponema denticola cystalysin. || 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. || 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(,). || Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. || Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase. || The role of Lys272 in the pyridoxal 5-phosphate active site of Synechococcus glutamate-1-semialdehyde aminotransferase. || 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. || Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene. || 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. || Identification of a common mutation in Finnish patients with nonketotic hyperglycinemia. || Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R. || Site-directed mutagenesis of the beta subunit of tryptophan synthase from Salmonella typhimurium. Role of active site glutamic acid 350. || Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. || Serine hydroxymethyltransferase: origin of substrate specificity. || The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate. || Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes. || Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction. || Effect of substitution of a lysyl residue that binds pyridoxal phosphate in thermostable D-amino acid aminotransferase by arginine and alanine. || 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. || 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. || Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase. || Structural and expression analyses of normal and mutant mRNA encoding glycine decarboxylase: three-base deletion in mRNA causes nonketotic hyperglycinemia. || 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. || The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. || Autonomous folding and coenzyme binding of the excised pyridoxal 5'-phosphate binding domain of aspartate aminotransferase from Escherichia coli. || Pyridoxal phosphate-dependent histidine decarboxylases. Cloning, sequencing, and expression of genes from Klebsiella planticola and Enterobacter aerogenes and properties of the overexpressed enzymes. || Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. || Aspartate aminotransferase with the pyridoxal-5'-phosphate-binding lysine residue replaced by histidine retains partial catalytic competence. || 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. || The environments of Trp-248 and Trp-330 in tryptophan indole-lyase from Escherichia coli. || 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. || Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli. || Characterization and expression of the complementary DNA encoding rat histidine decarboxylase. || The beta subunit of tryptophan synthase. Clarification of the roles of histidine 86, lysine 87, arginine 148, cysteine 170, and cysteine 230. || Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase. || [Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids. || Contribution of a conserved arginine near the active site of Escherichia coli D-serine dehydratase to cofactor affinity and catalytic activity. || Evidence that cysteine 298 is in the active site of tryptophan indole-lyase. || Site-directed mutagenesis of Petunia hybrida 5-enolpyruvyl- shikimate-3-phosphate synthase. Lys-23 is essential for substrate binding. || The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5'-phosphate produced by substitution of aspartic acid for glycine. || Serine hydroxymethyltransferase: mechanism of the racemization and transamination of D- and L-alanine || Substitution of an arginyl residue for the active site lysyl residue (Lys258) of aspartate aminotransferase. || Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis. || 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. || Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids. || Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme || Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1. || The molecular genetic basis of myophosphorylase deficiency (McArdle's disease). || A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype. || Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients. || Aminolevulinate synthase: lysine 313 is not essential for binding the pyridoxal phosphate cofactor but is essential for catalysis. || Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with gamma-thialysine. || beta-Cystathionase from Bordetella avium. Role(s) of lysine 214 and cysteine residues in activity and cytotoxicity. || Site-directed mutagenesis of His343-->Ala in Citrobacter freundii tyrosine phenol-lyase. Effects on the kinetic mechanism and rate-determining step. || The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations. || Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms. || Threonine dehydratases of Corynebacterium glutamicum with altered allosteric control: their generation and biochemical and structural analysis. || Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue. || Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site. || Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria. || Ligand-mediated changes in the tryptophan synthase indole tunnel probed by nile red fluorescence with wild type, mutant, and chemically modified enzymes. || Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells. || The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli. || The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase. || NMR studies of 1H resonances in the 10-18-ppm range for cytosolic aspartate aminotransferase. || NMR studies of 1H resonances in the 10-18-ppm range for aspartate aminotransferase from Escherichia coli. || Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system. || Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. || X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. || A visible marker for antisense mRNA expression in plants: inhibition of chlorophyll synthesis with a glutamate-1-semialdehyde aminotransferase antisense gene. || Shift in pH-rate profile and enhanced discrimination between dicarboxylic and aromatic substrates in mitochondrial aspartate aminotransferase Y70H. || Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. || 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. || Replacement of active-site lysine-239 of thermostable aspartate aminotransferase by S-(2-aminoethyl)cysteine: properties of the mutant enzyme. || Studies of the active-site lysyl residue of thermostable aspartate aminotransferase: combination of site-directed mutagenesis and chemical modification. || Function of the active-site lysine in Escherichia coli serine hydroxymethyltransferase. || Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors. || Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers. || Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog. || 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. || Determination of a functional lysine residue of a plant cysteine synthase bysite-directed mutagenesis, and the molecular evolutionary implications. || 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. || Role reversal for substrates and inhibitors. Slow inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors. || Molecular defect in a patient with pyridoxine-responsive homocystinuria. || Anaerobiosis and plant growth hormones induce two genes encoding 1-aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.). || The identification of a lysine residue reactive to pyridoxal-5-phosphate in the glycerol dehydrogenase from the thermophile Bacillus stearothermophilus. || Lysine 258 in aspartate aminotransferase. Enforcer of the circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift. || Mutant aspartate aminotransferase (K258H) without pyridoxal-5'-phosphate-binding lysine residue. Structural and catalytic properties. || A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase. || 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. || Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants. || A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene. || Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding. || Interaction of pyridoxal 5'-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase. || Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. || The mechanism of high-yielding chiral syntheses catalysed by wild-type and mutant forms of aspartate aminotransferase. || Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations. || Cloning of bovine muscle glycogen phosphorylase cDNA and identification of a mutation in cattle with myophosphorylase deficiency, an animal model for McArdle's disease. || Site-directed mutagenesis techniques in the study of Escherichia coli serine hydroxymethyltransferase. || 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. || Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. || Structural studies on folding intermediates of serine hydroxymethyltransferase using fluorescence resonance energy transfer. || Mutations at a glycine loop in aminolevulinate synthase affect pyridoxal phosphate cofactor binding and catalysis. || Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1. || Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients. || Cloning and analysis of the gene for cystathionine gamma-synthase from Arabidopsis thaliana. || 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. || Role of Arg-277 in the binding of pyridoxal 5'-phosphate to Trypanosoma brucei ornithine decarboxylase. || An anomalous side reaction of the Lys303 mutant aromatic L-amino acid decarboxylase unravels the role of the residue in catalysis. || Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria. || 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. || 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. || Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. || Importance of the amino terminus in maintenance of oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase. || Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99. || Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase. || 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. || Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation. || The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. || Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria. || Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558. || Role of arginine 439 in substrate binding of 5-aminolevulinate synthase. || Mutation analysis in myophosphorylase deficiency (McArdle's disease). || Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5'-phosphate cofactor. || Mutations in the liver glycogen phosphorylase gene (PYGL) underlying glycogenosis type VI. || The SPL1 tRNA splicing gene of Candida maltosa and Candida albicans. || Mutation of an active site residue of tryptophan synthase (beta-serine 377) alters cofactor chemistry. || Complementation analysis of mutants of 1-aminocyclopropane- 1-carboxylate synthase reveals the enzyme is a dimer with shared active sites. || Directed evolution of an aspartate aminotransferase with new substrate specificities. || Role of Arg-401 of cytosolic serine hydroxymethyltransferase in subunit assembly and interaction with the substrate carboxy group. || The role of lysine-256 in the structure and function of sheep liver recombinant serine hydroxymethyltransferase. || The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase. || Bacterial selenocysteine synthase--structural and functional properties. || Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate. || Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60. || Mutation of aspartate-233 to valine in mouse ornithine decarboxylase reduces enzyme activity. || Pyridoxal phosphate binding to wild type, W330F, and C298S mutants of Escherichia coli apotryptophanase: unraveling the cold inactivation. || Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination. || The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis. || Tryptophan synthase mutations that alter cofactor chemistry lead to mechanism-based inactivation. || The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8. || Transamination as a side-reaction catalyzed by alanine racemase of Bacillus stearothermophilus. || Isolation and characterization of ACC deaminase genes from two different plant growth-promoting rhizobacteria. || Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature. || Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. || Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase. || Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity. || Role of lysine 39 of alanine racemase from Bacillus stearothermophilus that binds pyridoxal 5'-phosphate. Chemical rescue studies of Lys39 --> Ala mutant.