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阿维巴坦与头孢他啶水解型 D 类β-内酰胺酶的相互作用。

Interactions between Avibactam and Ceftazidime-Hydrolyzing Class D β-Lactamases.

机构信息

Centre for Protein Engineering, University of Liège, B 4000 Liège, Belgium.

National Reference Laboratory for Monitoring of Antimicrobial Resistance in Gram-Negative Bacteria, CHU Dinant-Godinne, UCL Namur, B 5530 Yvoir, Belgium.

出版信息

Biomolecules. 2020 Mar 23;10(3):483. doi: 10.3390/biom10030483.

Abstract

Class D β-lactamases exhibit very heterogeneous hydrolysis activity spectra against the various types of clinically useful β-lactams. Similarly, and according to the available data, their sensitivities to inactivation by avibactam can vary by a factor of more than 100. In this paper, we performed a detailed kinetic study of the interactions between two ceftazidime-hydrolyzing OXA enzymes and showed that they were significantly more susceptible to avibactam than several other class D enzymes that do not hydrolyze ceftazidime. From a clinical point of view, this result is rather interesting if one considers that avibactam is often administered in combination with ceftazidime.

摘要

D 类 β-内酰胺酶对各种临床有用的β-内酰胺类药物的水解活性谱具有很大的异质性。同样,根据现有数据,它们对阿维巴坦失活的敏感性差异超过 100 倍。在本文中,我们对两种头孢他啶水解 OXA 酶之间的相互作用进行了详细的动力学研究,结果表明它们对阿维巴坦的敏感性明显高于其他几种不水解头孢他啶的 D 类酶。从临床的角度来看,如果考虑到阿维巴坦通常与头孢他啶联合使用,那么这一结果是非常有趣的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/e0a20dce2bf2/biomolecules-10-00483-g0A1.jpg

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