Studies on the Metabolism of Unsaturated Fatty Acids. VII. Separation and General Properties of Reduced Nicotinamide Adenine Dinucleotide Phosphate-dependent trans-2-Enoyl-Coenzyme A Reductase from Escherichia coli K-12
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概要
- 論文の詳細を見る
An enzyme fraction which catalyzes the reduction of trans-2-enoyl-coenzyme A (trans-2-enoyl-CoA) to the corresponding saturated acyl-CoA derivative was separated from Escherichia coli (E. coli) extracts. The enzyme utilized reduced nicotinamide adenine dinucleotide phosphate (NADPH) as a sole electron donor for the reduction of substrates, and it acted on acyl-CoA substrates, but not on acyl-carrier protein esters. Therefore, the name NADPH-dependent trans-2-enoyl-CoA reductase was proposed for this enzyme. The reductase was stable at around pH 7-8,and was active over a wide pH range between 6 and 9. It had a functional thiol group and was readily inhibited by thiol reagents such as p-hydroxymercuribenzoic acid, and by cupric and some other metal ions. The enzyme was induced when E. coli cells were cultured in a medium containing oleic acid. These results suggest that this reductase does not participate in the de novo synthesis of fatty acids but is a new enzyme, although its physiological role is uncertain at the present stage.
- 公益社団法人日本薬学会の論文
- 1982-07-25
著者
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水柿 道直
Pharmaceutical Institute Tohoku University
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山中 宏
Pharmaceutical Institute, Tohoku University
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白石 隆幸
Pharmaceutical Institute, Tohoku University
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西巻 知子
Pharmaceutical Institute, Tohoku University
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白石 隆幸
Laboratory Of Health Chemistry Niigata College Of Pharmacy
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西巻 知子
Pharmaceutical Institute Tohoku University
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