Cloning of a cDNA for short/branched chain acyl-Coenzyme A dehydrogenase from rat and characterization of its tissue expression and substrate specificity.
Zhang YX, Denoya CD, Skinner DD, Fedechko RW, McArthur HA, Morgenstern MR, Davies RA, Lobo S, Reynolds KA, Hutchinson CR
Title
Genes encoding acyl-CoA dehydrogenase (AcdH) homologues from Streptomyces coelicolor and Streptomyces avermitilis provide insights into the metabolism of small branched-chain fatty acids and macrolide antibiotic production.
A flavoprotein (FAD). The mammalian enzyme catalyses an oxidative reaction as a step in the mitochondrial beta-oxidation of short-chain 2-methyl fatty acids and participates in isoleucine degradation. The enzyme from the parasitic helminth Ascaris suum catalyses a reductive reaction as part of a fermentation pathway, shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA.
History
EC 1.3.8.5 created 1992 as EC 1.3.1.52, transferred 2012 to EC 1.3.8.5 (EC 1.3.99.12, created 1986, incorporated 2020), modified 2020
Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase.
Purification and characterization of the 2-methyl branched-chain Acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum.
Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F
Title
Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism.
Andresen BS, Christensen E, Corydon TJ, Bross P, Pilgaard B, Wanders RJ, Ruiter JP, Simonsen H, Winter V, Knudsen I, Schroeder LD, Gregersen N, Skovby F
Title
Isolated 2-methylbutyrylglycinuria caused by short/branched-chain acyl-CoA dehydrogenase deficiency: identification of a new enzyme defect, resolution of its molecular basis, and evidence for distinct acyl-CoA dehydrogenases in isoleucine and valine metabolism.
