Purification and characterization of α-keto amide reductase from Saccharomyces cerevisiae

被引：19
|
作者：
Ishihara, K
Yamamoto, H
Mitsuhashi, K
Nishikawa, K
Tsuboi, S
Tsujl, H
Nakajima, N
机构：
[1] Okayama Univ Sci, Dept Life Sci, Okayama 7000005, Japan
[2] Daicel Chem Ind Ltd, Tsukuba Res Ctr, CPI Co, Life Sci Dev Ctr, Tsukuba, Ibaraki 3050841, Japan
[3] Okayama Univ, Fac Environm Sci & Technol, Dept Environm Chem & Mat, Okayama 7008530, Japan
[4] Okayama Prefectural Univ, Grad Sch Hlth & Welf Sci, Soja, Okayama 7191197, Japan
来源：
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2004年 / 68卷 / 11期
关键词：
Saccharomyces cerevisiae; alpha-keto amide; alpha-keto ester; reduction; reductase;
D O I：
10.1271/bbb.68.2306
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：
An NADPH-dependent a-keto amide reductase was purified from Saccharomyces cerevisiae. The molecular mass of the native enzyme was estimated to be 33 and 36kDa by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The purified enzyme showed a reducing activity not only for aromatic alpha-keto amides but also for aliphatic and aromatic alpha-keto esters. The internal sequence of the enzyme was identical with that of a hypothetical protein (ORF YDL 124w) coded by yeast chromosome IV.
引用
收藏
页码：2306 / 2312
页数：7
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