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标题：Occurrence of a Novel L-2, 4-Diaminobutyrate Decarboxylase Activity in Some Species of Enterobacteriaceae, and Purification and Characterization of the Enzymes of Enterobacter aerogenes and Serratia marcescens
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作者：Shigeo YAMAMOTO ; Nobuo MUTOH ; Hisato IKAI 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：1996
卷号：19
期号：10
页码：1298-1303
DOI：10.1248/bpb.19.1298
出版社：The Pharmaceutical Society of Japan
摘要：L-2, 4-Diaminobutyrate decarboxylase (DABA DC) is a novel enzyme yielding 1, 3-diaminopropane (DAP) from DABA, which has previously been purified from strains of the genera Vibrio and Acinetobacter. In this study, wey also detected DABA DC activity in the species of Enterobacteriaceae : E. aerogenes, E. cloacae, E. agglomerans, Serratia marcescens, S. liquefaciens, Klebsiella pneumoniace, K. oxytoca and Citrobacter freundii, all of which produced DAP in sufficient amounts. Subsequently, the DABA DCs of E. aerogenes and S. marcescens were purified to homogeneity and characterized. Two separate enzymes had similar properties with respect to chromatographic behaviors, and were a dimer with subunits of identical molecular mass of about 51 kDa. The maximal activity of each enzyme was obtained at pH 8.0-8.25. Both enzymes required pyridoxal 5'-phosphate and Mg²⁺ for full activity, and were highly specific for L-DABA. There was immunological similarity, but not identity between these proteins, as determined by Ouchterlony double diffusion analysis with antiserum against the E. aerogenes DABA DC. They showed the same N-terminal amino acid sequence up to the 8th residue (S-K-L-N-P-I-L-A-). These enzymes were different in molecular mass, N-terminal amino acid sequence and antigenicity from DABA DCs of Acientobacter and Vibrio species.
关键词：L-2, 4-diaminobutyrate decarboxylase;1, 3-diaminopropane;Enterobacter aerogenes;Serratia marcescens;pyridoxal 5'-phosphate-dependent enzyme