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A further characterization of alanine dehydrogenase from Streptomyces aureofaciens
Author(s) -
Vančurová Ivana,
Vančura Aleš,
Volc Jindřich,
Neužil Jiří,
Běhal Vladislav
Publication year - 1989
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620290317
Subject(s) - nad+ kinase , chemistry , alanine , cofactor , biochemistry , streptomyces aureofaciens , oxidative deamination , dehydrogenase , nicotinamide adenine dinucleotide , serine , reductive amination , enzyme , stereochemistry , biology , amino acid , catalysis , streptomyces , bacteria , genetics
Homogeneous alanine dehydrogenase isolated from Streptomyces aureofaciens , a producer of tetracycline, was characterized from the point of its molecular and catalytic properties. Using analytical ultracentrifugation the molecular weight of alanine dehydrogenase was found to be 198,000. The enzyme could use as cofactors apart from NAD + also l,N 6 ‐etheno‐NAD + , 3‐acetylpyridine‐NAD + , deamino‐NAD + and nicotinamide guanine dinucleotide. The enzyme activity in the direction of oxidative deamination was not affected by the addition of nonsubstrate amino acids, however, it was sensitive to inhibitors of SH‐groups. Reductive amination of pyruvate was inhibited by L‐alanine, L‐serine and D‐alanine. The inhibition by L‐alanine and L‐serine was uncompetitive with respect to NADH and noncompetitive with regard to pyruvate and ammonium ions.