rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
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pubmed:dateCreated |
1984-2-14
|
pubmed:abstractText |
The interaction of 6 alpha-(temocillin) and 7 alpha-methoxy substituted (cefoxitin) beta-lactam compounds with various beta-lactamases was studied employing enzyme kinetics and compared to that of unsubstituted compounds. Both chromosomally mediated enzymes from Enterobacter cloacae and Citrobacter freundii were competitively inhibited by the methoxy-substituted compounds. Higher concentrations of cefoxitin caused a competitive inhibition of the plasmid-mediated Tem-1 enzyme, whereas temocillin led to a non-competitive inhibition of the Tem-1 enzyme. These results indicate that the discrepancies in the interaction on the above mentioned compounds have to be attributed to the different molecular structure of the beta-lactam nucleus. Moreover, no predictions can be made on the basis of an analogy between 6 alpha-methoxy-penams and 7 alpha-methoxy cephems.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
0176-6724
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
256
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
109-18
|
pubmed:dateRevised |
2009-6-8
|
pubmed:meshHeading |
pubmed-meshheading:6362278-Binding, Competitive,
pubmed-meshheading:6362278-Cefoxitin,
pubmed-meshheading:6362278-Cephalosporinase,
pubmed-meshheading:6362278-Cephalosporins,
pubmed-meshheading:6362278-Cephalothin,
pubmed-meshheading:6362278-Chromosomes, Bacterial,
pubmed-meshheading:6362278-Citrobacter,
pubmed-meshheading:6362278-Enterobacter,
pubmed-meshheading:6362278-Escherichia coli,
pubmed-meshheading:6362278-Kinetics,
pubmed-meshheading:6362278-Penicillinase,
pubmed-meshheading:6362278-Penicillins,
pubmed-meshheading:6362278-Plasmids,
pubmed-meshheading:6362278-Ticarcillin,
pubmed-meshheading:6362278-beta-Lactamases
|
pubmed:year |
1983
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pubmed:articleTitle |
Influence of methoxy-substitution of beta-lactam compounds on the interaction with various beta-lactamases.
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pubmed:publicationType |
Journal Article
|