Implication of Ile-69 and Thr-182 residues in kinetic characteristics of IRT-3 (TEM-32) beta-lactamase

Author:

Farzaneh S1,Chaibi E B1,Peduzzi J1,Barthelemy M1,Labia R1,Blazquez J1,Baquero F1

Affiliation:

1. URA 401 Centre National de la Recherche Scientifique,-MNHN, Quimper, France.

Abstract

The substitution of a methionine for an isoleucine at position 69 (Met69Ile), which causes inhibitor resistance to TEM-type beta-lactamases (IRT-3 and IRT-I69), altered the positions of the Asn-170 and Glu-166 side chains as well as the position of the catalytic water molecule. A novel hydrogen bond between the hydroxyl of Thr-182 and the carbonyl of Glu-64 was expected to be responsible for the increase in the catalytic activity of the IST-T182 and IRT-3 enzymes compared with those of TEM-1 and IRT-169, respectively.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference26 articles.

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3. Nucleotide sequence of the genes coding for the TEM-like ~-lactamases IRT-1 and IRT-2 (formerly called TRI-1 and TRI-2);Belaaouaj A.;FEMS Microbiol. Lett.,1994

4. Belaaouaj A. C. G. Vedel G. Paul L. Gilly A. Philippon and P. Névot. 1990. Beta-lactamase plasmidique de point isoélectrique 5.25 chez deux souches de Escherichia coli à spectre pénicillinase insensible aux inhibiteurs enzymatiques abstr. 91/C6. In Program and abstracts of the 10th Interdisciplinary Meeting on Anti-Infective Chemotherapy. Société Française de Microbiologie Paris France.

5. Characterization of new TEM-type ~-lactamase resistant to clavulanate, sulbactam, and tazobactam in a clinical isolate of Escherichia coli;Blazquez J.;Antimicrob. Agents Chemother.,1993

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