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

S Eaton, T Bursby, B Middleton, M Pourfarzam, K Mills, A W Johnson, K Bartlett

Journal: Biochemical Society transactions 2000;28(2):177-82

PMID: 10816122

Abstract

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'.

Address: Unit of Paediatric Surgery, Institute of Child Health, London, UK.

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