Studies on the metabolism of unsaturated fatty acids. X. Purification and some properties of 2,4-dienoyl-CoA reductase from Escherichia coli.
2,4-Dienoyl-CoA reductase has been separated from Escherichia coli grown in the presence of linoleic acid and purified to homogeneity. The enzyme has a molecular weight close to 50,000 as determined by gel filtration on Sephacryl S-200 Super-fine. The reductase was rather stable in a buffer containing citric acid and kept its full activity on heating at 55 degrees C for 10 min in the pH range of 5.5 to 6.5, but was completely inactivated on heating at 58 degrees C for 10 min. Phosphocellulose column chromatography revealed that the reductase was not involved in the multi-enzyme complex (molecular weight of 260,000) of fatty acid oxidation.
D004926:Escherichia coli / Q000201:enzymology*; D044943:Fatty Acid Desaturases / Q000302:isolation & purification* / Q000378:metabolism; D005231:Fatty Acids, Unsaturated / Q000378:metabolism*; D006358:Hot Temperature; D007700:Kinetics; D008970:Molecular Weight
D005231:Fatty Acids, Unsaturated; D044943:Fatty Acid Desaturases