Linked Life Data

2492417

Source:http://linkedlifedata.com/resource/pubmed/id/2492417

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-3-3
pubmed:abstractText
Stereospecificities of component enzymes in the pyruvate dehydrogenase complex and 2-ketoglutarate dehydrogenase complex from Escherichia coli for lipoate and dihydrolipoate are determined. Assays of the component enzymes using R,S-, R-, or S-lipoate or the enantiomers of dihydrolipoate show that only the R-enantiomers are substrates for these enzymes. Nonenzymatic reactions involving acetyl group transfer and coupled electron and acetyl group transfer between enantiomeric molecules of lipoate or/and dihydrolipoate proceed at significant rates. Coupled acetyl group and electron transfer from enzyme-bound acetyldihydrolipoyl moieties to free lipoate is also observed. The S-enantiomers are neither substrates nor inhibitors; however, products of S-enantiomers are slowly generated in enzymatic reactions owing to nonenzymatic reactions between enzyme-bound acetyldihydrolipoyl-groups and free S-lipoate or S-dihydrolipoate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
465-74
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
2-ketoacid dehydrogenase complexes of Escherichia coli: stereospecificities of the three components for (R)-lipoate.
pubmed:affiliation
Institute for Enzyme Research, Graduate School, University of Wisconsin, Madison 53705.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.