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pBR 322编码的RTEMβ-内酰胺酶与底物的相互作用。特定构象转变的证据。

Interaction of the pBR 322-coded RTEM beta-lactamase with substrates. Evidence for specific conformational transitions.

作者信息

Citri N, Zyk N

出版信息

Biochem J. 1982 Feb 1;201(2):425-7. doi: 10.1042/bj2010425.

Abstract

The rate of inactivation of RTEM-1 beta-lactamase by Pronase is accelerated by class A ('resistant') penicillins. Other substrates (class S penicillin and cephalosporins) protect against the inactivation. Cefoxitin, a semi-synthetic cephamycin, induces a more extensive, hysteretic response. In its presence the enzyme is inactivated by trypsin as well as by Pronase.

摘要

A类(“耐药”)青霉素可加速链霉蛋白酶对RTEM-1β-内酰胺酶的灭活速率。其他底物(S类青霉素和头孢菌素)则可防止其灭活。半合成头霉素头孢西丁会引发更广泛的滞后反应。在其存在的情况下,该酶不仅会被链霉蛋白酶灭活,还会被胰蛋白酶灭活。

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本文引用的文献

6
Mechanism of substrate-induced inactivation of beta-lactamase I.底物诱导β-内酰胺酶I失活的机制。
Eur J Biochem. 1980 Aug;109(2):575-80. doi: 10.1111/j.1432-1033.1980.tb04830.x.
9
Purification and properties of the gamma-type beta-lactamase of Bacillus cereus.
Arch Biochem Biophys. 1967 Sep;121(3):720-8. doi: 10.1016/0003-9861(67)90059-8.
10
Conformational adaptability in enzymes.酶的构象适应性
Adv Enzymol Relat Areas Mol Biol. 1973;37:397-648. doi: 10.1002/9780470122822.ch7.

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