Purification and Some Properties of NAD(P)H Dehydrogenase from Saccharomyces cerevisiae : Contribution to Glycolytic Methylglyoxal Pathway
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概要
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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 μM and 0.1 mM, respectively. The activity of the enzyme increased approximately 4-fold with Cu^<2+>. FAD, FMN and cytochrome c were not effective as electron acceptors, although Fe(CN)^<3->_6 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.
- 社団法人日本生物工学会の論文
- 1994-05-25
著者
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Inoue Yoshiharu
Research Institute For Food S-cience Kyoto University
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KIMURA AKIRA
Research Institute for Food Science, Kyoto University
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Kimura Akira
Research Institute For Food Science Kyoto University
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