title: Functional characterization of rat glutaryl-CoA dehydrogenase and its comparison with straight-chain acyl-CoA dehydrogenase.
abstract: Glutaryl-CoA dehydrogenase catalyzes the oxidative decarboxylation of the γ-carboxylate of the substrate, glutaryl-CoA, to yield crotonyl-CoA and CO(2). The enzyme is a member of the acyl-CoA dehydrogenase (ACD) family of flavoproteins. In the present study, the catalytic properties of this enzyme, including its substrate specificity, isomerase activity, and interactions with inhibitors, were systematically studied. Our results indicated that the enzyme has its catalytic properties very similar to those of short-chain and medium-chain acyl-CoA dehydrogenase except its additional decarboxylation reaction. Therefore, the inhibitors of fatty acid oxidation targeting straight chain acyl-CoA dehydrogenase could also function as inhibitors for amino acid metabolism of lysine, hydroxylysine, and tryptophan.
authors.affiliation: Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong, PR China.
authors.forename: Long
authors.initials: L
authors.lastname: Wu
authors.forename: Yuqin
authors.initials: Y
authors.lastname: Qiao
authors.forename: Jinbo
authors.initials: J
authors.lastname: Gao
authors.forename: Guisheng
authors.initials: G
authors.lastname: Deng
authors.forename: Wenhua
authors.initials: W
authors.lastname: Yu
authors.forename: Gong
authors.initials: G
authors.lastname: Chen
authors.forename: Ding
authors.initials: D
authors.lastname: Li
mesh_terms: D000214:Acyl Coenzyme A / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D004791:Enzyme Inhibitors / Q000494:pharmacology; D050770:Glutaryl-CoA Dehydrogenase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D051381:Rats; D013379:Substrate Specificity
chemical_list: D000214:Acyl Coenzyme A; D004791:Enzyme Inhibitors; D050770:Glutaryl-CoA Dehydrogenase