Linked Life Data

6427167

Source:http://linkedlifedata.com/resource/pubmed/id/6427167

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1984-7-12
pubmed:abstractText
The binding affinities of imipenem (N- formimidoylthienamycin ) to penicillin-binding proteins ( PBSs ) of Escherichia coli and Pseudomonas aeruginosa were determined by two different methods in which competition with [14C]benzylpenicillin for the binding sites was measured. By both methods imipenem was shown to have very high binding affinities to PBPs-2 and -4 in E. coli and P. aeruginosa, and appreciable affinities to most of their other major PBPs. But higher concentrations of imipenem were required for binding to the PBPs-3 in these bacteria. More direct information about the antibacterial activity of imipenem was obtained by measuring its inhibition of the peptidoglycan-synthetic enzyme activities of E. coli PBPs. The results of enzyme inhibitions were compatible with those obtained in binding experiments. The antibiotic inhibited the transpeptidase activities of PBPs-1A, -1B and -2, and the D-alanine carboxypeptidase activities of PBPs-4 and -5. The antibiotic also seemed to cause strong inhibition of the transglycosylase activity of PBP-1A by some unknown mechanism. It inhibited the transpeptidase activity of PBP-3 only weakly, which is consistent with the findings that it had low binding affinity to PBP-3 and did not inhibit septum formation by the cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Imipenem, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide..., http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Penicillins, http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases, http://linkedlifedata.com/resource/pubmed/chemical/Thienamycins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-8820
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
394-400
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Studies on the mechanism of action of imipenem (N-formimidoylthienamycin) in vitro: binding to the penicillin-binding proteins (PBPs) in Escherichia coli and Pseudomonas aeruginosa, and inhibition of enzyme activities due to the PBPs in E. coli.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't