Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1981-10-29
pubmed:abstractText
The steric course of the reaction catalyzed by Escherichia coli enoyl acyl-carrier-protein reductase was studied. 1. trans-2-[2-2H1]Decenoic and trans-2-[3-2H1]decenoic acids were synthesized and converted to the corresponding decenoyl thiol esters with CoA or acyl carrier protein. These deuterium-labeled decenoyl thiol esters were incubated with purified enoyl acyl-carrier-protein reductase in the presence of NADPH or NADH. 2. The unlabeled trans-2-decenoyl thiol esters were incubated with enoyl acyl-carrier-protein reductase in the presence of (4S)-[4-2H1]NADH. The unlabeled decenoyl thiol esters were also incubated with the enzyme in 2H2O. The decanoic acids formed in the above incubations were extracted and subjected to the action of acyl-CoA oxidase, which had been previously shown to catalyze the anti elimination of the pro-2R and pro-3R hydrogens of acyl-CoA. The resulting products, 2-decenoyl-CoAs, were converted to methyl esters and their deuterium contents were analyzed by gas chromatography/mass spectrometry. The results suggested that the reduction catalyzed by E. coli enoyl acyl-carrier-protein reductase occurs by a syn addition of hydrogen via a 2-Re, 3-Si attack on the double bond.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
116
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
581-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Steric course of reaction catalyzed by the enoyl acyl-carrier-protein reductase of Escherichia coli.
pubmed:publicationType
Journal Article