Human trifunctional protein deficiency: a new disorder of mitochondrial fatty acid beta-oxidation

Biochem Biophys Res Commun. 1992 Nov 16;188(3):1139-45. doi: 10.1016/0006-291x(92)91350-y.

Abstract

In this paper we report the identification of a new disorder of mitochondrial fatty acid beta-oxidation in a patient which presented with clear manifestations of a mitochondrial beta-oxidation disorder. Subsequent studies in fibroblasts revealed an impairment in palmitate beta-oxidation and in addition, a combined deficiency of long-chain enoyl-CoA hydratase, long-chain 3-hydroxyacyl-CoA-dehydrogenase and long-chain 3-oxoacyl-CoA thiolase. The recent identification of a multifunctional, membrane-bound beta-oxidation enzyme protein catalyzing all these three enzyme activities (Carpenter et al. (1992) Biochem. Biophys. Res. Commun. 183, 443-448; Uchida et al. (1992) J. Biol. Chem. 267, 1034-1041) suggested an underlying basis for this peculiar combination of three enzyme deficiencies. We show by means of size-exclusion chromatography that there is, indeed, a deficiency of the multifunctional beta-oxidation enzyme protein in this patient.

Publication types

  • Case Reports

MeSH terms

  • 3-Hydroxyacyl CoA Dehydrogenases / genetics
  • Acetyl-CoA C-Acyltransferase / genetics
  • Child, Preschool
  • Enoyl-CoA Hydratase / genetics
  • Fatty Acids / metabolism*
  • Fibroblasts / enzymology
  • Humans
  • Lipid Metabolism, Inborn Errors / metabolism*
  • Mitochondria / metabolism*
  • Molecular Weight
  • Multienzyme Complexes / genetics*
  • Oxidation-Reduction

Substances

  • Fatty Acids
  • Multienzyme Complexes
  • 3-Hydroxyacyl CoA Dehydrogenases
  • Acetyl-CoA C-Acyltransferase
  • Enoyl-CoA Hydratase