Biochemical Characterization of the FEZ-1 Metallo-β-Lactamase of Legionella gormanii ATCC 33297 T Produced in Escherichia coli-Reference-Cited by-同舟云学术

Biochemical Characterization of the FEZ-1 Metallo-β-Lactamase of Legionella gormanii ATCC 33297 T Produced in Escherichia coli

Published:2001-04 Issue:4 Volume:45 Page:1254-1262
ISSN:0066-4804
Container-title:Antimicrobial Agents and Chemotherapy
language:en
Short-container-title:Antimicrob Agents Chemother

Author:

Mercuri Paola Sandra¹,Bouillenne Fabrice¹,Boschi Letizia²,Lamotte-Brasseur Josette¹,Amicosante Gianfranco³,Devreese Bart⁴,van Beeumen Jozef⁴,Frère Jean-Marie¹,Rossolini Gian Maria²,Galleni Moreno¹

Affiliation:

1. Centre d'Ingénierie des Protéines, Université de Liège, B-4000 Liège,1 and

2. Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università di Siena, I-53100 Siena, 2 and

3. Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, I-67100 Coppito, L'Aquila,3 Italy

4. Laboratorium voor Eiwitbiochemie en Eiwitengineering, University of Gent, B-9000 Gent,4 Belgium, and

Abstract

ABSTRACT The bla FEZ-1 gene coding for the metallo-β-lactamase of Legionella (Fluoribacter) gormanii ATCC 33297 T was overexpressed via a T7 expression system in Escherichia coli BL21(DE3)(pLysS). The product was purified to homogeneity in two steps with a yield of 53%. The FEZ-1 metallo-β-lactamase exhibited a broad-spectrum activity profile, with a preference for cephalosporins such as cephalothin, cefuroxime, and cefotaxime. Monobactams were not hydrolyzed. The β-lactamase was inhibited by metal chelators. FEZ-1 is a monomeric enzyme with a molecular mass of 29,440 Da which possesses two zinc-binding sites. Its zinc content did not vary in the pH range of 5 to 9, but the presence of zinc ions modified the catalytic efficiency of the enzyme. A model of the FEZ-1 three-dimensional structure was built.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Link

https://journals.asm.org/doi/pdf/10.1128/AAC.45.4.1254-1262.2001

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