RGD Reference Report - The mitochondrial trifunctional protein: centre of a beta-oxidation metabolon? - Rat Genome Database

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The mitochondrial trifunctional protein: centre of a beta-oxidation metabolon?

Authors: Eaton, S  Bursby, T  Middleton, B  Pourfarzam, M  Mills, K  Johnson, AW  Bartlett, K 
Citation: Eaton S, etal., Biochem Soc Trans. 2000 Feb;28(2):177-82.
RGD ID: 2317625
Pubmed: PMID:10816122   (View Abstract at PubMed)

The trifunctional enzyme comprises three consecutive steps in the mitochondrial beta-oxidation of long-chain acyl-CoA esters: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-ketoacyl-CoA thiolase. Deficiencies in either 3-hydroxyacyl-CoA dehydrogenase activity, or all three activities, are important causes of human disease. The dehydrogenase and thiolase have a requirement for NAD+ and CoA respectively, whose levels are conserved within the mitochondrion and thus provide possible means for control and regulation of beta-oxidation. Using analysis of the intact CoA ester intermediates produced by the complex, we have examined the sensitivity of the complex to NAD+/NADH and acetyl-CoA. We consider the evidence for channelling within the trifunctional protein and propose a model for a beta-oxidation 'metabolon'.

Molecular Pathway Annotations    Click to see Annotation Detail View

RGD Manual Annotations

Objects Annotated

Genes (Rattus norvegicus)
Hadha  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha)
Hadhb  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta)

Genes (Mus musculus)
Hadha  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha)
Hadhb  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta)

Genes (Homo sapiens)
HADHA  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha)
HADHB  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta)


Additional Information