Antibiotic recognition by binuclear metallo-β-lactamases revealed by X-ray crystallography

J Spencer, J Read, RB Sessions, S Howell… - Journal of the …, 2005 - ACS Publications
Metallo-β-lactamases are zinc-dependent enzymes responsible for resistance to β-lactam
antibiotics in a variety of host bacteria, usually Gram-negative species that act as opportunist …

Metallo-β-lactamase: structure and mechanism

Z Wang, W Fast, AM Valentine, SJ Benkovic - Current opinion in chemical …, 1999 - Elsevier
This past year has produced determinations of X-ray crystal structures for three metallo-β-
lactamases and the elucidation of the catalytic mechanisms for a monozinc and a dizinc …

Metallo-β-lactamases: does it take two to tango?

JA Cricco, EG Orellano, RM Rasia… - Coordination chemistry …, 1999 - Elsevier
Metallo-β-lactamases are a subset of zinc hydrolases able to hydrolyze the β-lactam ring of
several antibiotics. The number of structural and mechanistic studies on these …

The Mechanisms of Catalysis by Metallo β‐Lactamases

MI Page, A Badarau - Bioinorganic chemistry and applications, 2008 - Wiley Online Library
Class B β‐lactamases or metallo‐β‐lactamases (MBLs) require zinc ions to catalyse the
hydrolysis of β‐lactam antibiotics such as penicillins, cephalosporins, carbapenems, and …

A variety of roles for versatile zinc in metallo-β-lactamases

AI Karsisiotis, CF Damblon, GCK Roberts - Metallomics, 2014 - academic.oup.com
Metallo-β-lactamases are important as a major source of resistance of pathogenic bacteria
to the widely used β-lactam antibiotics. They show considerable diversity in terms of …

Metallo-β-lactamases: novel weaponry for antibiotic resistance in bacteria

MW Crowder, J Spencer, AJ Vila - Accounts of chemical research, 2006 - ACS Publications
Metallo-β-lactamases are broad-spectrum zinc enzymes, able to inactivate most clinically
useful β-lactam antibiotics. Their structural and functional diversity has thus far limited the …

Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-β-lactamases

JM Gonzalez, A Buschiazzo, AJ Vila - Biochemistry, 2010 - ACS Publications
Subclass B1 β-lactamases are Zn (II)-dependent hydrolases that confer bacterial resistance
to most clinically useful β-lactam antibiotics. The enzyme BcII from Bacillus cereus is a …

Metallo‐β‐lactamase structure and function

T Palzkill - Annals of the New York Academy of Sciences, 2013 - Wiley Online Library
β‐Lactam antibiotics are the most commonly used antibacterial agents and growing
resistance to these drugs is a concern. Metallo‐β‐lactamases are a diverse set of enzymes …

Role of the Zn1 and Zn2 sites in Metallo-β-lactamase L1

Z Hu, G Periyannan, B Bennett… - Journal of the American …, 2008 - ACS Publications
In an effort to probe the role of the Zn (II) sites in metallo-β-lactamase L1, mononuclear metal
ion containing and heterobimetallic analogues of the enzyme were generated and …

Metallo-β-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily

C Bebrone - Biochemical pharmacology, 2007 - Elsevier
One strategy employed by bacterial strains to resist β-lactam antibiotics is the expression of
metallo-β-lactamases requiring Zn2+ for activity. In the last few years, many new zinc β …