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. 1994 Dec;60(12):4630–4633. doi: 10.1128/aem.60.12.4630-4633.1994

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

Tetsuji Nakamura 1,*, Toru Nagasawa 2, Fujio Yu 1, Ichiro Watanabe 1, Hideaki Yamada 3,†
PMCID: PMC202036  PMID: 16349472

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.

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Selected References

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