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TEM-2分子模型显示的额外离子键可能会导致TEM-1和TEM-2β-内酰胺酶催化特性出现细微差异。

An additional ionic bond suggested by molecular modelling of TEM-2 might induce a slight discrepancy between catalytic properties of TEM-1 and TEM-2 beta-lactamases.

作者信息

Chaïbi E B, Farzaneh S, Péduzzi J, Barthélémy M, Labia R

机构信息

Muséum National Histoire Naturelle, CNRS URA 401, Paris, France.

出版信息

FEMS Microbiol Lett. 1996 Oct 1;143(2-3):121-5. doi: 10.1111/j.1574-6968.1996.tb08470.x.

Abstract

The plasmid-mediated TEM-1 and TEM-2 beta-lactamases are the most commonly encountered among Gram-negative bacteria. They belong to molecular class A, and differ by one amino acid at position 39:TEM-1 have a glutamine and TEM-2 a lysine. Kinetic parameters (kcat and Km) and catalytic efficiency (kcat/Km) of TEM-1 and TEM-2 beta-lactamases are slightly, but significantly different. For all antibiotics except methicillin and cefazolin, the catalytic efficiency values of TEM-2 are clearly greater than that of TEM-1. Molecular modelling of TEM-2, when compared to that of TEM-1, showed an additional ionic bond between Lys-39 and Glu-281.

摘要

质粒介导的TEM-1和TEM-2β-内酰胺酶是革兰氏阴性菌中最常见的。它们属于A类分子,在第39位氨基酸处相差一个氨基酸:TEM-1有一个谷氨酰胺,TEM-2有一个赖氨酸。TEM-1和TEM-2β-内酰胺酶的动力学参数(kcat和Km)以及催化效率(kcat/Km)略有不同,但差异显著。对于除甲氧西林和头孢唑林以外的所有抗生素,TEM-2的催化效率值明显高于TEM-1。与TEM-1相比,TEM-2的分子模型显示赖氨酸-39和谷氨酸-281之间存在一个额外的离子键。

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