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PMID: 8891161 Published · ppublish English Journal Article

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

Antimicrobial agents and chemotherapy ·Vol. 40 ·No. 10 ·1996-10-00 ·Pages 2434-6

Farzaneh S, Chaibi EB, Peduzzi J, Barthelemy M, Labia R, Blazquez J, Baquero F

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.

MeSH Terms
Catalysis Cephalosporins/metabolism Isoleucine/chemistry,metabolism Kinetics Penicillins/metabolism Threonine/chemistry,metabolism beta-Lactamases/chemistry,metabolism
Chemicals
Cephalosporins Penicillins Isoleucine Threonine beta-lactamase IRT-3 beta-Lactamases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Farzaneh S
URA 401 Centre National de la Recherche Scientifique,-MNHN, Quimper, France.
Chaibi E B
Peduzzi J
Barthelemy M
Labia R
Blazquez J
Baquero F
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20 references, click to expand
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Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
Published
1996-10-00
Pages
2434-6
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC163551
Subset
IM
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