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2-Methylbutyryl CoA dehydrogenase from mitochondria of Ascaris suum and its relationship to NADH-dependent 2-methylcrotonyl CoA reduction.

Acyl CoA dehydrogenase and electron-transfer flavoprotein have been isolated and partially purified from mitochondria of the anaerobic nematode, Ascaris suum. 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.[1]

References

  1. 2-Methylbutyryl CoA dehydrogenase from mitochondria of Ascaris suum and its relationship to NADH-dependent 2-methylcrotonyl CoA reduction. Komuniecki, R., Fekete, S., Thissen, J. Biochem. Biophys. Res. Commun. (1984) [Pubmed]
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