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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1996-3-27
|
| pubmed:abstractText |
Escherichia coli TEM1 is a penicillinase and belongs to class A beta-lactamases. Its naturally occurring mutants are responsible for bacterial resistance to beta-lactamin-based antibiotics. X-ray structure determinations show that all class A beta-lactamases are similar, but, despite the numerous kinetic investigations, the reaction mechanism of these enzymes is still debated. We address the questions of what the molecular contexts during the acylation and deacylation steps are and how they contribute to the efficiency of these penicillinases.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0969-2126
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
603-13
|
| pubmed:dateRevised |
2008-8-22
|
| pubmed:meshHeading |
pubmed-meshheading:8590021-Acylation,
pubmed-meshheading:8590021-Aspartic Acid,
pubmed-meshheading:8590021-Bacterial Proteins,
pubmed-meshheading:8590021-Binding Sites,
pubmed-meshheading:8590021-Catalysis,
pubmed-meshheading:8590021-Crystallography, X-Ray,
pubmed-meshheading:8590021-Electrochemistry,
pubmed-meshheading:8590021-Mutagenesis, Site-Directed,
pubmed-meshheading:8590021-Substrate Specificity,
pubmed-meshheading:8590021-beta-Lactamases
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Electrostatic analysis of TEM1 beta-lactamase: effect of substrate binding, steep potential gradients and consequences of site-directed mutations.
|
| pubmed:affiliation |
Laboratoire de Pharmacologie et de Toxicologie Fondamentales du CNRS, Toulouse, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|