期刊
EUROPEAN JOURNAL OF BIOCHEMISTRY
卷 269, 期 9, 页码 2394-2402出版社
BLACKWELL PUBLISHING LTD
DOI: 10.1046/j.1432-1033.2002.02899.x
关键词
phenylacetaldehyde reductase; NADH regeneration; chiral alcohol; asymmetric reduction; Corynebacterium sp.
Phenylacetaldehyde reductase (PAR) produced by styrene-assimilating Corynebacterium strain ST-10 was used to synthesize chiral alcohols. This enzyme with a broad substrate range reduced various prochiral aromatic ketones and beta-ketoesters to yield optically active secondary alcohols with an enantiomeric purity of more than 98% enantiomeric excess (e.e.). The Escherichia coli recombinant cells which expressed the par gene could efficiently produce important pharmaceutical intermediates; (R)-2-chloro-1-(3-chlorophenyl)ethanol (28 mg.mL(-1)) from m -chlorophenacyl chloride, ethyl (R)-4-chloro-3-hydroxy butanoate) (28 mg.mL(-1)) from ethyl 4-chloro-3-oxobutanoate and (S)-N-tert -butoxycarbonyl(Boc)-3-pyrrolidinol from N -Boc-3-pyrrolidinone (51 mg.mL(-1)), with more than 86% yields. The high yields were due to the fact that PAR could concomitantly reproduce NADH in the presence of 3-7% (v/v) 2-propanol in the reaction mixture. This biocatalytic process provided one of the best asymmetric reductions ever reported.
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