Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes

Perham, R.N. and Jones, D.D. and Chauhan, H.J. and Howard, M.J. (2002) Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes. Biochemical Society Transactions, 30 (2). pp. 47-51. ISSN 0300-5127. (The full text of this publication is not available from this repository)

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Abstract

Heteronuclear NMR spectroscopy and other experiments indicate that the true substrate of the E1 component of 2-oxo acid dehydrogenase complexes is not lipoic acid but the lipoyl domain of the E2 component. E1 can recognize the lipoyl-lysine residue as such, but reductive acylation ensues only if the domain to which the lipoyl group is attached is additionally recognized by virtue of a mosaic of contacts distributed chiefly over the half of the domain that contains the lipoyl-lysine residue. The lipoyl-lysine residue may not be freely swinging, as supposed hitherto, but may adopt a preferred orientation pointing towards a nearby loop on the surface of the lipoyl domain. This in turn may facilitate the insertion of the lipoyl group into the active site of E1, where reductive acylation is to occur. The results throw new light on the concept of substrate channelling and active-site coupling in these giant multifunctional catalytic machines.

Item Type: Article
Additional information: Journal Article Research Support, Non-U.S. Gov't Review England
Uncontrolled keywords: lipoic acid; lipoyl domain; protein-protein interaction; pyruvate dehydrogenase
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Mark Howard
Date Deposited: 09 Sep 2008 16:46
Last Modified: 14 Jan 2010 14:20
Resource URI: http://kar.kent.ac.uk/id/eprint/5353 (The current URI for this page, for reference purposes)
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