来自面包酵母的两种L-立体选择性羰基还原酶的蛋白质结构差异及催化功能相似性

Differences in protein structure and similarities in catalytic function of two L-stereoselective carbonyl reductases from bakers' yeast.

作者信息

Nakajima N, Ishihara K, Kondo S, Tsuboi S, Utaka M, Nakamura K

机构信息

Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins 80523.

出版信息

Biosci Biotechnol Biochem. 1994 Nov;58(11):2080-1. doi: 10.1271/bbb.58.2080.

DOI:10.1271/bbb.58.2080

Abstract

We purified and studied two L-stereoselective carbonyl reductases from bakers' yeast (Saccharomyces cerevisiae). One catalyzed exclusively the enantioselective reduction of carbonyl compounds such as beta-keto esters and the other acted on alpha-acetoxy ketones and beta-keto esters. The enzymes had identical molecular weights and catalyzed the L-stereoselective reduction of various carbonyl compounds with similar substrate specificity, but they were different proteins coded by different genes.

摘要

我们从面包酵母（酿酒酵母）中纯化并研究了两种L-立体选择性羰基还原酶。一种专门催化羰基化合物如β-酮酯的对映选择性还原，另一种作用于α-乙酰氧基酮和β-酮酯。这两种酶具有相同的分子量，并且以相似的底物特异性催化各种羰基化合物的L-立体选择性还原，但它们是由不同基因编码的不同蛋白质。

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