Linked Life Data

9105408

Source:http://linkedlifedata.com/resource/pubmed/id/9105408

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-5-1
pubmed:abstractText
We previously identified and purified UDP-glucuronosyltransferase (UGT) isoforms as targets of protein acylation from rat liver microsomes (Yamashita et al., Biochem J 312: 301-308, 1995). The acylation of UGT isoforms occurred upon incubation with acyl-CoA without another protein acyltransferase, suggesting that it was autoacylation. The study revealed the interaction of UGT isoforms with acyl-CoA. In the present study, the effects of fatty acyl-CoA on UGT activities were examined thoroughly, using a rat liver microsomal and purified enzyme fractions. The UGT activities of both fractions were inhibited by acyl-CoA in a concentration-dependent manner. The effect of acyl-CoA was observed on the activities toward various substrates, suggesting that the effect shows the wide spectrum of the isoforms of UGT. To assess the mechanism underlying the inhibition of UGT activity by acyl-CoA, the relationship of the inhibition, acyl-CoA binding to the proteins, and changes in the tertiary structure of the enzyme were examined. The kinetics of these phenomena were related closely with each other. Furthermore, the inhibition of UGT activity was specified for acyl-CoA, though a structurally related compound, acyl-3-dephosphoCoA, had no inhibitory effect. The results suggested that the specific binding of acyl-CoA to UGT isoforms induced conformational changes of the enzymes and resultant inhibition of UGT activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
561-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Inhibition of UDP-glucuronosyltransferase activity by fatty acyl-CoA. Kinetic studies and structure-activity relationship.
pubmed:affiliation
Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't