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

Sedigheh Farzaneh | Zendy; El Bachir Chaibi | Zendy; Jean Péduzzi | Zendy; Michel Barthélémy | Zendy; Roger Labia | Zendy; Jesús Blázquez | Zendy; Fernando Baquero | Zendy

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

Author(s) -

Sedigheh Farzaneh,

El Bachir Chaibi,

Jean Péduzzi,

Michel Barthélémy,

Roger Labia,

Jesús Blázquez,

Fernando Baquero

Publication year - 1996

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.40.10.2434

Subject(s) - isoleucine , chemistry , enzyme , methionine , stereochemistry , catalysis , side chain , hydrogen bond , beta (programming language) , molecule , biochemistry , amino acid , organic chemistry , leucine , polymer , computer science , programming language

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.

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