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来自耳炎假单胞菌的POM-1金属β-内酰胺酶的生化特性

Biochemical characterization of the POM-1 metallo-β-lactamase from Pseudomonas otitidis.

作者信息

Borgianni Luisa, De Luca Filomena, Thaller Maria Cristina, Chong Yunsop, Rossolini Gian Maria, Docquier Jean-Denis

机构信息

Dipartimento di Biotecnologie Mediche, Università di Siena, Siena, Italy.

Dipartimento di Biologia, Università di Roma Tor Vergata, Rome, Italy.

出版信息

Antimicrob Agents Chemother. 2015 Mar;59(3):1755-8. doi: 10.1128/AAC.03843-14. Epub 2014 Dec 15.

DOI:10.1128/AAC.03843-14
PMID:25512428
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4325775/
Abstract

The POM-1 metallo-β-lactamase is a subclass B3 resident enzyme produced by Pseudomonas otitidis, a pathogen causing otic infections. The enzyme was overproduced in Escherichia coli BL21(DE3), purified by chromatography, and subjected to structural and functional analysis. The purified POM-1 is a tetrameric enzyme of broad substrate specificity with higher catalytic activities with penicillins and carbapenems than with cephalosporins.

摘要

POM-1金属β-内酰胺酶是由耳炎假单胞菌产生的B3亚类常驻酶，耳炎假单胞菌是一种引起耳部感染的病原体。该酶在大肠杆菌BL21(DE3)中过量表达，通过色谱法纯化，并进行结构和功能分析。纯化后的POM-1是一种具有广泛底物特异性的四聚体酶，对青霉素和碳青霉烯类的催化活性高于头孢菌素类。

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