Studies on the Metabolism of Unsaturated Fatty Acids. II. Separation and General Properties of Reduced Nicotinamide Adenine Dinucleotide Phosphate dependent cis-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 cis-2-alkenoyl-Coenzyme A (-CoA) to the corresponding saturated acyl-CoA derivatives has been separated from Escherichia coli extracts. The enzyme catalyzes the reduction of cis-2-octenoyl-CoA with an apparent Michaelis-Menten constant of 2.0×10^<-5>M in the presence of reduced nicotinamide adenine dinucleotide phosphate (NADPH), but not in the presence of reduced nicotinamide adenine dinucleotide (NADH). The reductase is inactive on cis-3- or trans-2-isomers. The reductase is stable at 45°, but its activity is lost on heating at 55° for 10 min. Some other properties of this enzyme are also described.
- 公益社団法人日本薬学会の論文
- 1979-10-25
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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鵜沼 恒夫
Pharmaceutical Institute, Tohoku University
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鵜沼 恒夫
Pharmaceutical Institute Tohoku University
関連論文
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