beta-Oxidation enzymes in fibroblasts from patients with 3-hydroxydicarboxylic aciduria

Pediatr Res. 1994 Jul;36(1 Pt 1):111-4. doi: 10.1203/00006450-199407001-00020.

Abstract

The activities of 3-hydroxyacyl-CoA dehydrogenase, enoyl-CoA hydratase, and 3-ketoacyl-CoA thiolase were measured in fibroblasts from eight patients with 3-hydroxydicarboxylic aciduria. Measurement of 3-hydroxyacyl-CoA dehydrogenase with 3-ketopalmitoyl-CoA as substrate provided conclusive evidence for a deficiency of the long-chain 3-hydroxyacyl-CoA dehydrogenase in seven of the patients. Measurement of the enzyme in the normal direction cannot be recommended because this gives a higher residual activity. A trifunctional enzyme protein is responsible for the 3-hydroxyacyl-CoA dehydrogenase as well as for the hydratase and thiolase activities. A slight decrease in one or both of the other two activities was observed in four of the seven deficient patients, indicating that a defect in the trifunctional enzyme protein may affect the three enzyme activities to different degrees.

Publication types

  • Clinical Trial
  • Controlled Clinical Trial
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Hydroxyacyl CoA Dehydrogenases / metabolism*
  • Acetyl-CoA C-Acyltransferase / metabolism*
  • Cells, Cultured
  • Enoyl-CoA Hydratase / metabolism*
  • Female
  • Fibroblasts / enzymology
  • Humans
  • Male
  • Metabolism, Inborn Errors / enzymology
  • Metabolism, Inborn Errors / urine*
  • Oxidation-Reduction

Substances

  • 3-Hydroxyacyl CoA Dehydrogenases
  • Acetyl-CoA C-Acyltransferase
  • Enoyl-CoA Hydratase