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2-Methylbutyryl CoA dehydrogenase from mitochondria of Ascarissuum and its relationship to NADH-dependent 2-methylcrotonyl CoA reduction
Authors:Richard Komuniecki  Steven Fekete  Julia Thissen
Institution:Department of Biology, University of Toledo Toledo, Ohio, USA
Abstract:Acyl CoA dehydrogenase and electron-transfer flavoprotein have been isolated and partially purified from mitochondria of the anaerobic nematode, Ascarissuum. Dehydrogenase activity was greatest with 2-methylbutyryl CoA and the relative substrate specificities of the ascarid dehydrogenase(s) differ greatly from their mammalian counterparts. It appears that the ascarid dehydrogenase functions physiologically as a reductase, catalyzing the final step in the synthesis of branched-chain fatty acids. In fact, incubations of A. suum mitochondrial membranes with electron-transfer flavoprotein, 2-methylbutyryl CoA dehydrogenase, 2-methylcrotonyl CoA and NADH resulted in a substantial, rotenone-sensitive, 2-methylbutyrate synthesis. These results suggest that the ascarid electron-transport chain and at least two soluble mitochondrial proteins are involved in the NADH-dependent reduction of 2-methylcrotonyl CoA.
Keywords:ETF  electron transfer flavoprotein  2-MB  2-methylbutyrate  2-MV  2-methylvalerate
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