PURIFICATION AND CHARACTERIZATION OF 2 EPOXIDE HYDROLASES FROM CORYNEBACTERIUM SP STRAIN-N-1074

被引:31
作者
NAKAMURA, T
NAGASAWA, T
YU, FJ
WATANABE, I
YAMADA, H
机构
[1] NAGOYA UNIV,DEPT APPL BIOL SCI,CHIKUSA KU,NAGOYA,AICHI 464,JAPAN
[2] KYOTO UNIV,DEPT AGR CHEM,SAKYO KU,KYOTO 606,JAPAN
关键词
D O I
10.1128/AEM.60.12.4630-4633.1994
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Enzymes IIa and IIb, which catalyze the conversion of epichlorohydrin (ECH) to 3-chloro-1,2-propanediol (MCP), were purified from Corynebacterium sp. strain N-1074, which catalyzes the formation of (A)-MCP from prochiral 1,3-dichloro-2-propanol via ECH. The specific activity of enzyme IIa for the formation of MCP from ECH was about 6.4-fold higher than that of enzyme IIb. Both enzymes catalyzed the conversion of 1,2-epoxides to the corresponding diol, although they differed in several enzymatic properties.
引用
收藏
页码:4630 / 4633
页数:4
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