DIFFERENCES IN PROTEIN-STRUCTURE AND SIMILARITIES IN CATALYTIC FUNCTION OF 2 L-STEREOSELECTIVE CARBONYL REDUCTASES FROM BAKERS-YEAST

被引：14

作者：

NAKAJIMA, N

ISHIHARA, K

KONDO, S

TSUBOI, S

UTAKA, M

NAKAMURA, K

机构：

[1] OKAYAMA PREFECTURAL UNIV, DEPT NUTR SCI, OKAYAMA 71911, JAPAN

[2] OKAYAMA UNIV, FAC ENGN, DEPT APPL CHEM, OKAYAMA 700, JAPAN

[3] KYOTO UNIV, CHEM RES INST, UJI, KYOTO 611, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1994年 / 58卷 / 11期

关键词：

D O I：

10.1271/bbb.58.2080

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2080 / 2081

页数：2

共 15 条

[1] ALDOSE REDUCTASE AND RHO-CRYSTALLIN BELONG TO THE SAME PROTEIN SUPERFAMILY AS ALDEHYDE REDUCTASE [J].