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

Implication of Ile-69 and Thr-182 residues in kinetic characteristics of IRT-3 (TEM-32) beta-lactamase
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Ile-69 和 Thr-182 残基对 IRT-3 (TEM-32) β-内酰胺酶动力学特征的影响

DOI:
10.1128/aac.40.10.2434
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发表时间:
1996
影响因子:
4.9
通讯作者:
F. Baquero
F. Baquero
中科院分区:
医学2区
文献类型:
--
作者:
S. Farzaneh;E. B. Chaibi;J. Péduzzi;M. Barthélémy;R. Labia;J. Blázquez;F. Baquero

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在位置69(Met 69 Ile)处用甲硫氨酸取代异亮氨酸导致抑制剂对TEM型β-内酰胺酶(IRT-3和IRT-I69)的抗性,改变了Asn-170和Glu-166侧链的位置以及催化水分子的位置。与TEM-1和IRT-169相比,IST-T182和IRT-3酶的催化活性分别增加了,这与Thr-182的羟基和Glu-64的羰基之间的新型氢键有关。
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.
一种产生具有改变酶性质的蛋白质的有效方法:应用于β-内酰胺酶。
DOI: 10.1073/pnas.86.23.9094
发表时间: 1989
影响因子: 11.1
作者:
Oliphant,AR;Struhl,K
通讯作者: Struhl,K