S. Farzaneh et al., IMPLICATION OF ILE-69 AND THR-182 RESIDUES IN KINETIC CHARACTERISTICSOF IRT-3 (TEM-32) BETA-LACTAMASE, Antimicrobial agents and chemotherapy, 40(10), 1996, pp. 2434-2436
The substitution of a methionine for an isoleucine at position 69 (Met
69IIe), 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 catal
ytic activity of the IST-T182 and IRT-3 enzymes compared with those of
TEM-1 and IRT-I69, respectively.