Linked Life Data

8132614

Source:http://linkedlifedata.com/resource/pubmed/id/8132614

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1994-4-21
pubmed:abstractText
Analysis of inhibitor studies indicates that carnitine palmitoyltransferase-I has two separate sites for inhibitor binding. One site is located on the cytoplasmic side of the mitochondrial outer membrane. Malonyl-CoA, the most important physiological inhibitor of carnitine palmitoyltransferase-I, binds primarily to this site, but it can also bind to another site. A second inhibitory site is located at the active site of carnitine palmitolytransferase-I. Coenzyme A, a product/inhibitor of carnitine palmitoyltransferase-I binds primarily at this site and can inhibit carnitine palmitoyltransferase-I at physiological concentrations, but can also attenuate malonyl-CoA inhibition. Analogs of malonyl-CoA and other simpler compounds containing two carbonyl groups but no coenzyme A moiety inhibit only at the cytoplasmic site, indicating that this site has an absolute requirement for two carbonyl groups but has no absolute requirement for a coenzyme A moiety. Inhibitors acting through the active site included the active-site-directed inhibitor (+)-hemipalmitoylcarnitinium. These studies support the existence of two regulatory binding sites for the control of hepatic fatty acid oxidation: (a) the active site, for regulation by the inhibitory binding of coenzyme A and acetyl-CoA, and (b) a separate regulatory malonyl-CoA-binding site that is physical separated from the active site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8803-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Yonetani-Theorell analysis of hepatic carnitine palmitoyltransferase-I inhibition indicates two distinct inhibitory binding sites.
pubmed:affiliation
Department of Pharmacology, College of Medicine, University of Tennessee, Memphis 38163.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't