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Purification and Characterization of Two Epoxide Hydrolases from Corynebacterium sp. Strain N-1074

By Tetsuji Nakamura, Toru Nagasawa, Fujio Yu, Ichiro Watanabe and Hideaki Yamada

Abstract

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 (R)-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

Topics: Enzymology and Protein Engineering
Year: 1994
OAI identifier: oai:pubmedcentral.nih.gov:202036
Provided by: PubMed Central
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