beta-Oxidation enzymes in fibroblasts from patients with 3-hydroxydicarboxylic aciduria.
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.
Venizelos
N
N
Department of Clinical Chemistry, Karolinska Institute, Huddinge University Hospital, Sweden.
Ijlst
L
L
Wanders
R J
RJ
Hagenfeldt
L
L
D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism*; D000102:Acetyl-CoA C-Acyltransferase / Q000378:metabolism*; D002478:Cells, Cultured; D004746:Enoyl-CoA Hydratase / Q000378:metabolism*; D005260:Female; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D008297:Male; D008661:Metabolism, Inborn Errors / Q000201:enzymology / Q000652:urine*; D010084:Oxidation-Reduction
D015094:3-Hydroxyacyl CoA Dehydrogenases; D000102:Acetyl-CoA C-Acyltransferase; D004746:Enoyl-CoA Hydratase