Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus: purification and characterization
作者： Y. Asano , A. Nakazawa , K. Endo
DOI: 10.1016/S0021-9258(18)61119-6
关键词:
摘要: NAD+-dependent phenylalanine dehydrogenases were purified 1,500- and 1,600-fold, crystallized from Sporosarcina ureae SCRC-R04 Bacillus sphaericus SCRC-R79a, respectively. The enzymes homogeneous as judged by disc gel electrophoresis. enzyme S. has a molecular weight of 305,000, while that B. 340,000. Each is probably composed eight subunits identical in weight. showed high substrate specificity the oxidative deamination reaction acting on L-phenylalanine, acted L-phenylalanine L-tyrosine. had lower specificities reductive amination alpha-keto acids. phenylpyruvate, alpha-ketocaproate, alpha-keto-gamma-methylthiobutyrate rho-hydroxyphenylpyruvate. rho-hydroxyphenylpyruvate, alpha-keto-gamma-methylthiobutyrate. catalyzes transfer pro-S (B) hydrogen NADH.
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