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

被引：39

作者：

Farzaneh, S

Chaibi, EB

Peduzzi, J

Barthelemy, M

Labia, R

Blazquez, J

Baquero, F

机构：

[1] MNHN,CNRS,UMR 175,F-29000 QUIMPER,FRANCE

[2] MNHN,CNRS,URA 401,F-29000 QUIMPER,FRANCE

[3] HOSP RAMON Y CAJAL,E-28034 MADRID,SPAIN

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 1996年 / 40卷 / 10期

关键词：

D O I：

10.1128/AAC.40.10.2434

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The substitution of a methionine for an isoleucine at position 69 (Met69IIe), 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-I69, respectively.

引用

页码：2434 / 2436

页数：3

共 26 条

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