Abstract
The substitution of a methionine for an isoleucine at position 69 (Met69Ile), which causes inhibitor resistance to TEM-type β-lactamases (IRT- 3 and IRT-169), 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-TI82 and IRT-3 enzymes compared with those of TEM-1 and IRT-169, respectively.
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CITATION STYLE
Farzaneh, S., Chaibi, E. B., Peduzzi, J., Barthelemy, M., Labia, R., Blazquez, J., & Baquero, F. (1996). Implication of Ile-69 and Thr-182 residues in kinetic characteristics of IRT-3 (TEM-32) β-lactamase. Antimicrobial Agents and Chemotherapy, 40(10), 2434–2436. https://doi.org/10.1128/aac.40.10.2434
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