A NOVEL NADPH-DEPENDENT CARBONYL REDUCTASE OF CANDIDA-MACEDONIENSIS - PURIFICATION AND CHARACTERIZATION

被引：36

作者：

KATAOKA, M ^{[1
]}

DOI, Y ^{[1
]}

SIM, TS ^{[1
]}

SHIMIZU, S ^{[1
]}

YAMADA, H ^{[1
]}

机构：

[1] KYOTO UNIV,DEPT AGR CHEM,SAKYO KU,KYOTO 606,JAPAN

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1992年 / 294卷 / 02期

基金：

日本学术振兴会;

关键词：

D O I：

10.1016/0003-9861(92)90713-7

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：

A novel NADPH-dependent carbonyl reductase was purified to homogeneity from the soluble fraction of a cell extract of Candida macedoniensis AKU 4588. The enzyme catalyzes not only the reduction of quinones, but also the reduction of aromatic aldehydes, conjugated polyketones, 2′-ketopantothenate esters, and 4-chloro-3-oxobutanoate esters. The enzyme shows absolute specificity for NADPH as a coenzyme and also shows quite high affinity toward NADPH (Km < 5 μm). The apparent Km values for menadione and p-toluquinone are 167 and 180 μm, respectively. The enzyme is not a flavoprotein and is a monomer protein with a relative molecular mass of 45,000. Dicoumarol, quercetin, and some sulfhydryl reagents inhibit the enzyme activity. © 1992.

引用

页码：469 / 474

页数：6

共 25 条

[1] GEL-FILTRATION BEHAVIOUR OF PROTEINS RELATED TO THEIR MOLECULAR WEIGHTS OVER A WIDE RANGE [J].