Linked Life Data

3580384

Source:http://linkedlifedata.com/resource/pubmed/id/3580384

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-7-6
pubmed:abstractText
The characteristic green colour of native short-chain acyl-CoA dehydrogenases (EC 1.3.99.2) results from a charge transfer complex between the FAD prosthetic group and a tightly bound molecule of CoA-persulphide. The native enzyme from ox liver mitochondria was found to have about 60% of its FAD cofactor liganded with CoA-persulphide. When artificially fully liganded with CoA-persulphide, this enzyme was inhibited by 90% in comparison to unliganded enzyme. Enzymic activity could be slowly restored by displacing the CoA-persulphide with high concentrations of butyryl-CoA, the enzyme's physiological substrate. The results show that CoA-persulphide is a potent inhibitor of short-chain acyl-CoA dehydrogenase and may have a physiological role in the regulation of beta-oxidation.
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
2
pubmed:volume
919
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't