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Article

Properties of IRT-14 (TEM-45), a newly characterized mutant of TEM-type beta-lactamases.

Antimicrobial agents and chemotherapy - 1 Feb 1997

Caniça M M, Barthélémy M, Gilly L, Labia R, Krishnamoorthy R, Paul G

Abstract excerpt

IRT-14 (TEM-45) is a new mutant TEM-type beta-lactamase that was isolated from clinical Escherichia coli P37 and that confers resistance to broad-spectrum penicillins with reduced sensitivity to beta-lactamase inhibitors. The MICs of amoxicillin alone and of amoxicillin combined with 2 micrograms of clavulanic acid or 2 micrograms of tazobactam per ml were 4,096, 2,048, and 1,024 micrograms/ml, respectively. The...

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Identifiers

PMID: 9021194
DOI: 10.1128/AAC.41.2.374
PMCID: PMC163716

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Related research

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Research trail→

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Properties of IRT-14 (TEM-45), a newly characterized mutant of TEM-type beta-lactamases.PMID 9021194Read ↗

Molecular characterization of TEM-59 (IRT-17), a novel inhibitor-resistant TEM-derived beta-lactamase in a clinical isolate of Klebsiella oxytoca.Semantic proximity Read ↗

TEM-109 (CMT-5), a natural complex mutant of TEM-1 beta-lactamase combining the amino acid substitutions of TEM-6 and TEM-33 (IRT-5).Semantic proximity Read ↗

Characterization of a new TEM-derived beta-lactamase produced in a Serratia marcescens strain.Semantic proximity Read ↗

A complex mutant of TEM-1 beta-lactamase with mutations encountered in both IRT-4 and extended-spectrum TEM-15, produced by an Escherichia coli clinical isolate.Semantic proximity Read ↗

A β-lactamase inhibitory protein mutant displays high potency and a broad inhibition profile due to an altered binding mode with β-lactamases.Semantic proximity Read ↗

Evolution of TEM-type enzymes: biochemical and genetic characterization of two new complex mutant TEM enzymes, TEM-151 and TEM-152, from a single patient.Semantic proximity Read ↗

Characterization of a new TEM-type beta-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli.Semantic proximity Read ↗

Phenotypic study of resistance of beta-lactamase-inhibitor-resistant TEM enzymes which differ by naturally occurring variations and by site-directed substitution at Asp276.Semantic proximity Read ↗

Construction and characterization of mutants of the TEM-1 beta-lactamase containing amino acid substitutions associated with both extended-spectrum resistance and resistance to beta-lactamase inhibitors.Semantic proximity Read ↗

Val-237 for Ala substitution in the TEM-2 beta-lactamase dramatically alters the catalytic efficiencies towards carbenicillin and ticarcillin.Semantic proximity Read ↗

Kinetic Study of Laboratory Mutants of NDM-1 Metallo-β-Lactamase and the Importance of an Isoleucine at Position 35.Semantic proximity Read ↗

TEM-121, a novel complex mutant of TEM-type beta-lactamase from Enterobacter aerogenes.Semantic proximity Read ↗

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