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

  • Farzaneh S
  • Chaibi E
  • Peduzzi J
 et al. 
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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.

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Authors

  • Sedigeh Farzaneh

  • El Bachir Chaibi

  • Jean Peduzzi

  • Michel Barthelemy

  • Roger Labia

  • Jesus Blazquez

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