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Chemical modification of cysteine residues of L-methionine γ-lyase
The L-methionine γ-lyase of Pseudomonas putida contains 16 cysteinyl residues per mol of enzyme, which is composed of four identical polypeptide chains. Eight of these residues are buried inside theExpand
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Properties of α-Amino-ε-caprolactam Racemase from Achromobacter obae
α-Amino-e-caprolactam racemase, which occurs in the cytoplasmic fraction of Achromobacter obae, has been purified to homogeneity. It has a monomeric structure with a molecular weight of approximatelyExpand
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Leucine dehydrogenase of a thermophilic anaerobe, Clostridium thermoaceticum: gene cloning, purification and characterization
The leucine dehydrogenase (L-leucine: NAD+ oxidoreductase, deaminating, EC gene of Clostridium thermoaceticum was cloned and expressed in Escherichia coli C600 with a vector plasmid,Expand
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Synthesis of Selenocystine and Selenohomocystine with O-Acetylhomoserine Sulfhydrylase
We describe here the synthesis of selenium amino acids with O-acetylhomoserine sulfhydrylase, partially purified from baker’s yeast. The enzyme was found to catalyze the synthesis of l-selenocystineExpand
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Biotransformation of Oleic Acid by Micrococcus luteus Cells
We isolated bacterial strains tolerant to high concentrations of oleic acid from soil samples, and studied biotransformation of fatty acids with the bacteria. We found that a strain BL0–3 identifiedExpand
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Racemization of α-Amino-δ-valerolactam Catalyzed by α-Aminog-ε-caprolactam Racemase from Achromobacter obae
(1983). Racemization of α-Amino-δ-valerolactam Catalyzed by α-Amino-∊-caprolactam Racemase from Achromobacter obae. Agricultural and Biological Chemistry: Vol. 47, No. 5, pp. 1149-1150.
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Inactivation of Amino Acid Racemase by S-(N-Methylthiocarbamoyl)- D, L-cysteine
S-(N-Methylthiocarbamoyl)-d- and l--cysteine (MTCC) are new irreversible inhibitors of the amino acid racemase from Pseudomonas putida. Interactions between d- or l-MTCC and purified amino acidExpand
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