Linked Life Data

3719003

Source:http://linkedlifedata.com/resource/pubmed/id/3719003

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-7-28
pubmed:abstractText
Rates of carnitine palmitoyltransferase-catalyzed conversion of palmitoylcarnitine to palmitoyl-CoA are markedly decreased with the progress of this reaction presumably owing to the build up of inhibitory palmitoyl-CoA in the enzyme vicinity. High, above micellar, concentrations of palmitoylcarnitine, phosphatidylcholine liposomes and high KCl concentrations increased the activity, apparently by facilitating the removal of palmitoyl-CoA from the enzyme surface. The presence of cardiolipin was found to be inhibitory. The enzyme activity followed in the direction of palmitoylcarnitine formation with low palmitoyl-CoA concentration as substrate, was inhibited by phosphatidylcholine, but stimulated by cardiolipin. Both of these lipids markedly stimulated the enzyme activity followed by the isotope exchange procedure which requires progression of both the forward and the backward reactions. The results indicate that one of the effects of phospholipids on carnitine palmitoyltransferase activity is exerted from the ability of these substances to bind the amphipathic reactants of this enzyme, particularly long-chain acyl-CoA. The possibility that the activity of the membrane-bound carnitine palmitoyltransferase may at times be affected by changes in the concentrations and composition of the various phospholipids in the enzyme's vicinity is raised by these findings.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
877
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
223-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Differential effects of phosphatidylcholine and cardiolipin on carnitine palmitoyltransferase activity.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, Non-U.S. Gov't