2,6-Dimethylheptanoyl-CoA is a specific substrate for long-chain acyl-CoA dehydrogenase (LCAD): evidence for a major role of LCAD in branched-chain fatty acid oxidation

Biochim Biophys Acta. 1998 Jul 31;1393(1):35-40. doi: 10.1016/s0005-2760(98)00053-8.

Abstract

Oxidation of straight-chain fatty acids in mitochondria involves the complicated interaction between a large variety of different enzymes. So far four different mitochondrial straight-chain acyl-CoA dehydrogenases have been identified. The physiological function of three of the four acyl-CoA dehydrogenases has been resolved in recent years especially from studies on patients suffering from certain inborn errors of mitochondrial fatty acid beta-oxidation. The physiological role of long-chain acyl-CoA dehydrogenase (LCAD) has remained obscure, however. The results described in this paper provide strong evidence suggesting that LCAD plays a central role in branched-chain fatty acid metabolism since it turns out to be the major acyl-CoA dehydrogenase reacting with 2,6-dimethylheptanoyl-CoA, a metabolite of pristanic acid, which itself is the alpha-oxidation product of phytanic acid.

MeSH terms

  • Acyl-CoA Dehydrogenase, Long-Chain / deficiency
  • Acyl-CoA Dehydrogenase, Long-Chain / metabolism*
  • Cells, Cultured
  • Coenzyme A / metabolism*
  • Fatty Acids / metabolism*
  • Humans
  • Mitochondria / metabolism
  • Oxidation-Reduction
  • Oxidoreductases / metabolism
  • Oxidoreductases Acting on CH-CH Group Donors*
  • Substrate Specificity

Substances

  • 2,6-dimethylheptanoyl-CoA
  • Fatty Acids
  • Oxidoreductases
  • Oxidoreductases Acting on CH-CH Group Donors
  • Acyl-CoA Dehydrogenase, Long-Chain
  • 2-methylacyl-CoA dehydrogenase
  • Coenzyme A