Linked Life Data

7018565

Source:http://linkedlifedata.com/resource/pubmed/id/7018565

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1981-9-25
pubmed:abstractText
The interaction of the RTEM beta-lactamase with two derivatives of olivanic acid has been studied. The compound MM22382 (1) behaves simply as a good substrate for the enzyme and is a relatively ineffective inhibitor. In contrast, the sulfate ester MM13902 (2) is a poor substrate and an excellent inhibitor of the enzyme. The inhibition derives from a branching of the normal hydrolytic pathway of the enzyme. At long times, all the catalytic activity of the enzyme returns. Free sulfate ion is not produced during the interaction with the enzyme, which rules out a mechanistic pathway involving beta elimination between C-6 and C-8. The validity of a number of alternative schemes is assessed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2732-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Inhibition of the RTEM beta-lactamase from Escherichia coli. Interaction of enzyme with derivatives of olivanic acid.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.