PURIFICATION AND SOME PROPERTIES OF NAD(P)H DEHYDROGENASE FROM SACCHAROMYCES-CEREVISIAE - CONTRIBUTION TO GLYCOLYTIC METHYLGLYOXAL PATHWAY

被引:4
作者
INOUE, Y
KIMURA, A
机构
[1] Research Institute for Food Science, Kyoto University, Uji, Kyoto
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1994年 / 77卷 / 05期
关键词
D O I
10.1016/0922-338X(94)90129-5
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
NAD(P)H dehydrogenase was purified approximately 480-fold from Saccharomyces cerevisiae with 6.5% activity yield. The enzyme was homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be 40,000-44,000 by gel filtration on Sephadex G-150 column chromatography and SDS-polyacrylamide gel electrophoresis. The K(m) values for NADPH and NADH were 7.3 muM and 0.1 mM, respectively. The activity of the enzyme increased approximately 4-fold with Cu2+. FAD, FMN and cytochrome c were not effective as electron acceptors, although Fe(CN)(6)3- was slightly effective. NADH generated by the reaction of lactaldehyde dehydrogenase in the glycolytic methylglyoxal pathway will be reoxidized by NAD(P)H dehydrogenase. NAD(P)H dehydrogenase thus may contribute to the reduction/oxidation system in the glycolytic methylglyoxal pathway to maintain the flux of methylglyoxal to lactic acid via lactaldehyde.
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页码:557 / 561
页数:5
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