Intact alpha-subunit is required for membrane-binding of human mitochondrial trifunctional beta-oxidation protein, but is not necessary for conferring 3-ketoacyl-CoA thiolase activity to the beta-subunit

M J Weinberger; P Rinaldo; A W Strauss; M J Bennett

doi:10.1006/bbrc.1995.1468

Intact alpha-subunit is required for membrane-binding of human mitochondrial trifunctional beta-oxidation protein, but is not necessary for conferring 3-ketoacyl-CoA thiolase activity to the beta-subunit

Biochem Biophys Res Commun. 1995 Apr 6;209(1):47-52. doi: 10.1006/bbrc.1995.1468.

Authors

M J Weinberger¹, P Rinaldo, A W Strauss, M J Bennett

Affiliation

¹ Department of Pathology, University of Texas Southwestern Medical Center at Dallas 75235, USA.

PMID: 7726862
DOI: 10.1006/bbrc.1995.1468

Abstract

We have studied the activities of alpha and beta subunit enzymes of the beta-oxidation trifunctional protein complex in a patient who does not process the alpha-subunit. Long-chain 3-ketoacyl-CoA thiolase, the beta-subunit enzyme, was transported into the mitochondrial matrix, where it expressed normal levels of activity, but was not translocated to the membrane. Thus, intact alpha-subunit is required for trifunctional protein membrane translocation, but is not necessary for conferring activity of the beta-subunit.

MeSH terms

3-Hydroxyacyl CoA Dehydrogenases / deficiency
3-Hydroxyacyl CoA Dehydrogenases / metabolism
Acetyl-CoA C-Acyltransferase / metabolism*
Cells, Cultured
Humans
Infant, Newborn
Intracellular Membranes / metabolism
Lipid Metabolism, Inborn Errors / metabolism
Liver / cytology
Liver / enzymology
Male
Mitochondria / metabolism*
Mitochondrial Trifunctional Protein
Multienzyme Complexes / metabolism*
Protein Binding
Skin / cytology
Skin / metabolism

Substances

Multienzyme Complexes
3-Hydroxyacyl CoA Dehydrogenases
Acetyl-CoA C-Acyltransferase
Mitochondrial Trifunctional Protein