Systematic investigation of Saccharomyces cerevisiae enzymes catalyzing carbonyl reductions

被引：168

作者：

Kaluzna, WA ^{[1
]}

Matsuda, T ^{[1
]}

Sewell, AK ^{[1
]}

Stewart, JD ^{[1
]}

机构：

[1] Univ Florida, Dept Chem, Gainesville, FL 32611 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 40期

关键词：

D O I：

10.1021/ja0469479

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Eighteen key reductases from baker's yeast (Saccharomyces cerevisiae) have been overproduced in Escherichia coli as glutathione S-transferase fusion proteins. A representative set of alpha- and beta-keto esters was tested as substrates (11 total) for each purified fusion protein. The stereoselectivities of beta-keto ester reductions depended both on the identity of the enzyme and the substrate structure, and some reductases yielded both L- and D-alcohols with high stereoselectivities. While a-keto esters were generally reduced with lower enantioselectivities, it was possible in all but one case to identify pairs of yeast reductases that delivered both alcohol antipodes in optically pure form. Taken together, the results demonstrate not only that individual yeast reductases can be used to supply important chiral building blocks, but that GST-fusion proteins allow rapid identification of synthetically useful biocatalysts (along with their corresponding genes).

引用

页码：12827 / 12832

页数：6

共 33 条

[21] Asymmetric synthesis of β-hydroxy esters and α-alkyl-β-hydroxy esters by recombinant Escherichia coli expressing enzymes from baker's yeast [J].