抄録
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 2.0×10-5M 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.
