D-hydroxyacyl-CoA dehydrogenase deficiency. Identification of a new peroxisomal disorder with implications for other disorders of beta-oxidation.
The second and third steps of peroxisomal beta-oxidation are catalysed by two multifunctional enzymes: D-bifunctional protein and L-bifunctional protein. Here we show that fibroblasts of a patient described as being deficient in the 3-hydroxyacyl-CoA dehydrogenase component of D-bifunctional protein and fibroblasts of a patient described as being deficient in L-bifunctional protein do not complement one another. Using a newly developed method to measure the activity of D-bifunctional protein in fibroblast homogenates, we found that the activity of the D-bifunctional protein was completely deficient in the patient with presumed L-bifunctional protein deficiency.
van Grunsven
E G
EG
University of Amsterdam, Dept. of Clinical Chemistry, The Netherlands.
van Berkel
E
E
Denis
S
S
Mooijer
P A
PA
Wanders
R J
RJ
D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000172:deficiency*; D002478:Cells, Cultured; D004746:Enoyl-CoA Hydratase / Q000172:deficiency*; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D007535:Isomerases; D009097:Multienzyme Complexes / Q000172:deficiency*; D010084:Oxidation-Reduction; D063994:Peroxisomal Bifunctional Enzyme; D018901:Peroxisomal Disorders / Q000175:diagnosis* / Q000201:enzymology*
D009097:Multienzyme Complexes; D015094:3-Hydroxyacyl CoA Dehydrogenases; C576253:EHHADH protein, human; D004746:Enoyl-CoA Hydratase; D063994:Peroxisomal Bifunctional Enzyme; D007535:Isomerases