Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase.
The stereochemical course of dehydrogenation catalyzed by acyl-CoA oxidase was investigated using the enzymes from rat liver peroxisomes and Candida lipolytica. Stearoyl-CoA and nonanoyl-CoA, stereospecifically labeled with deuterium at either C-2 or C-3, were incubated with the enzyme, the products were converted to methyl esters and their deuterium contents were measured by gas chromatography-mass spectrometry. The results suggested that acyl-CoA oxidase-catalyzed dehydrogenation occurred by anti-elimination of the pro 2R and pro-3R hydrogens of acyl-CoA.
D000214:Acyl Coenzyme A / Q000378:metabolism; D042962:Acyl-CoA Oxidase; D000818:Animals; D002175:Candida / Q000201:enzymology; D055598:Chemical Phenomena; D002621:Chemistry; D044943:Fatty Acid Desaturases / Q000378:metabolism*; D008401:Gas Chromatography-Mass Spectrometry; D008099:Liver / Q000201:enzymology; D008968:Molecular Conformation; D010088:Oxidoreductases / Q000378:metabolism*; D051381:Rats
D000214:Acyl Coenzyme A; D010088:Oxidoreductases; D044943:Fatty Acid Desaturases; D042962:Acyl-CoA Oxidase