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由大肠杆菌产生的CMY-2的Tyr199Cys突变形式CMY-107对肟基-β-内酰胺的水解作用增强。

Increased Hydrolysis of Oximino-β-Lactams by CMY-107, a Tyr199Cys Mutant Form of CMY-2 Produced by Escherichia coli.

作者信息

Kotsakis S D, Miriagou V, Vetouli E E, Bozavoutoglou E, Lebessi E, Tzelepi E, Tzouvelekis L S

机构信息

Laboratory of Bacteriology, Hellenic Pasteur Institute, Athens, Greece

Department of Biopathology, A. & P. Kyriakou Children's Hospital, Athens, Greece.

出版信息

Antimicrob Agents Chemother. 2015 Dec;59(12):7894-8. doi: 10.1128/AAC.01793-15. Epub 2015 Oct 5.

DOI:10.1128/AAC.01793-15
PMID:26438499
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4649145/
Abstract

The cephalosporinase CMY-107, a Tyr199Cys mutant form of CMY-2 encoded by an IncI self-transferable plasmid carried by an Escherichia coli clinical strain, was characterized. The enzyme hydrolyzed oximino-cephalosporins and aztreonam more efficiently than CMY-2 did.

摘要

头孢菌素酶CMY-107是由一株大肠杆菌临床菌株携带的IncI自我转移质粒编码的CMY-2的Tyr199Cys突变形式，对其进行了特性分析。该酶比CMY-2更有效地水解肟基头孢菌素和氨曲南。

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