Takashi Osumi, T. Hashimoto
Jul 28, 1978
Citations
2
Influential Citations
198
Citations
Quality indicators
Journal
Biochemical and biophysical research communications
Abstract
Abstract Acyl-CoA oxidase was purified from rat liver based on the palmitoyl-CoA-dependent H2O2-forming activity. Enoyl-CoA formation from palmitoyl-CoA by this enzyme was shown by the following observations; first, palmitoyl-CoA-dependent NAD+ reduction in the presence of this enzyme, crotonase, and 3-hydroxyacyl-CoA dehydrogenase, and, second, palmitoyl-CoA-dependent increase in absorbance at 263 nm. Same amounts of enoyl-CoA and H2O2 were formed during the reaction. It is concluded that this enzyme catalyzes the following reaction: Palmitoyl-CoA + O2 → transm -2-Hexadecenoyl-CoA + H2O2. It was most active toward C12-C18 acyl-CoAs. C20 and C22 acyl-CoAs were also oxidized, but C4 and C6 acyl-CoAs were hardly oxidized at all.