Biochemical characterization of the acquired metallo-β-lactamase SPM-1 from Pseudomonas aeruginosa

被引：57

作者：

Murphy, TA ^{[1
]}

Simm, AM

Toleman, MA

Jones, RN

Walsh, TR

机构：

[1] Univ Bristol, Dept Pathol & Microbiol, Bristol BS8 1TD, Avon, England

[2] JMI Labs, JONES Grp, N Liberty, IA USA

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2003年 / 47卷 / 02期

关键词：

D O I：

10.1128/AAC.47.2.582-587.2003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

SPM-1 is a new metallo-beta-lactamase recently identified in Pseudomonas aeruginosa strain 48-1997A, isolated in Sao Paulo, Brazil. Kinetic analysis demonstrated that SPM-1 has a broad hydrolytic profile across a wide range of beta-lactam antibiotics. Considerable variation was observed within the penicillin, cephalosporin, and carbapenem subfamilies; however, on the whole, SPM-1 appears to preferentially hydrolyze cephalosporins. The highest k(cat)K(m) ratios (in micromolar per second) overall were observed for this subgroup. The hydrolytic profile of SPM-1 bears the most similarity to that of the metallo-beta-lactamase IMP-1, yet for the most part, SPM-1 has k(cat)/K-m values higher than those of IMP-1. Zinc chelator studies established that progressive inhibition of SPM-1 by EDTA, dipicolinic acid, and 1-10-o-phenanthroline demonstrated a biexponential pattern in which none of the chelators completely inhibited SPM-1. A homology model of SPM-1 was developed on the basis of the IMP-1 crystal structure, which showed the protein folding and active-site structure characteristic of metallo-beta-lactamases and which provides an explanation for the kinetic profiles observed.

引用

页码：582 / 587

页数：6

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