CHARACTERIZATION OF ALDEHYDE REDUCTASE OF SPOROBOLOMYCES-SALMONICOLOR

被引：52

作者：

KATAOKA, M

SAKAI, H

MORIKAWA, T

KATOH, M

MIYOSHI, T

SHIMIZU, S

YAMADA, H

机构：

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

[2] DENKI KAGAKU KOGYO CO,RES CTR,DEPT BIOCHEM,TOKYO,JAPAN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1122卷 / 01期

关键词：

ALDEHYDE REDUCTASE; ALDOSE REDUCTASE; ALDO-KETO REDUCTASE; (S-SALMONICOLOR);

D O I：

10.1016/0167-4838(92)90127-Y

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 aldehyde reductase (EC 1.1.1.2) isolated from Sporobolomyces salmonicolor AKU 4429 was further characterized. The enzyme also catalyzed the reductions of D-glucuronate, D-glucose, D-xylose and D-galactose at high concentrations. K(m) values for D-glucuronate and D-glucose are 345 and 4270 mM, respectively. Quercetin, dicoumarol and some SH-reagents inhibited the enzyme activity. NH2-terminal amino acid sequence analysis showed that the S. salmonicolor enzyme is partially the same as the aldo-keto reductase family proteins in primary protein structure.

引用

页码：57 / 62

页数：6

共 31 条

[1] PRODUCTION OF 2-KETO-L-GULONATE, AN INTERMEDIATE IN L-ASCORBATE SYNTHESIS, BY A GENETICALLY MODIFIED ERWINIA-HERBICOLA [J].