Implication of a peroxisomal enzyme in the catabolism of glutaryl-CoA

Abstract

A linear rate of H2O2 production is found when glutaryl-CoA is incubated with liver homogenates. This enzyme activity is termed glutaryl-CoA oxidase. Its main characteristics are described and compared with those of glutaryl-CoA dehydrogenase (EC 1.3.99.7) and palmitoyl-CoA oxidase (EC 1.1.3.-). The latter enzyme catalyzes the 1st step of peroxisomal .beta.-oxidation. Glutaryl-CoA oxidase shares several properties with palmitoyl-CoA oxidase. The activities of both enzymes in mouse liver are increased by feeding the animals with a clofibrate-containing diet. Subcellular fractionation of the liver homogenates on a linear sucrose gradient indicates that glutaryl-CoA oxidase is a peroxisomal enzyme.