Linked Life Data

12023822

Source:http://linkedlifedata.com/resource/pubmed/id/12023822

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-5-23
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0300-5127
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes.
pubmed:affiliation
Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, U.K. r.n.perham@bioc.cam.ac.uk
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't