Metallo-β-lactamases: two binding sites for one catalytic metal ion?

U Heinz, HW Adolph - Cellular and Molecular Life Sciences CMLS, 2004 - Springer
During the past few years the results from molecular biological, biochemical, chemical,
physical and theoretical approaches expanded the knowledge about metallo-β-lactamases …

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 …

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 …

Ebselen as a potent covalent inhibitor of New Delhi metallo-β-lactamase (NDM-1)

E Wai-chiáChan - Chemical communications, 2015 - pubs.rsc.org
We report the discovery of a promising NDM-1 inhibitor, ebselen, through a cell-based
screening approach. Enzymatic kinetic study and ESI-MS analysis suggested that ebselen …

Metallo-β-lactamase inhibitors by bioisosteric replacement: Preparation, activity and binding

S Skagseth, S Akhter, MH Paulsen… - European journal of …, 2017 - Elsevier
Bacterial resistance is compromising the use of β-lactam antibiotics including carbapenems.
The main resistance mechanism against β-lactams is hydrolysis of the β-lactam ring …

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 …

The metallo-β-lactamase GOB is a mono-Zn (II) enzyme with a novel active site

J Moran-Barrio, JM Gonzalez, MN Lisa… - Journal of Biological …, 2007 - ASBMB
Metallo-β-lactamases (MβLs) are zinc-dependent enzymes able to hydrolyze and inactivate
most β-lactam antibiotics. The large diversity of active site structures and metal content …

Molecular basis of NDM-1, a new antibiotic resistance determinant

Z Liang, L Li, Y Wang, L Chen, X Kong, Y Hong, L Lan… - PLoS …, 2011 - journals.plos.org
The New Delhi Metallo-β-lactamase (NDM-1) was first reported in 2009 in a Swedish
patient. A recent study reported that Klebsiella pneumonia NDM-1 positive strain or …

NDM-4 metallo-β-lactamase with increased carbapenemase activity from Escherichia coli

P Nordmann, AE Boulanger… - Antimicrobial agents and …, 2012 - Am Soc Microbiol
ABSTRACT A clinical Escherichia coli isolate resistant to all β-lactams, including
carbapenems, expressed a novel metallo-β-lactamase (MBL), NDM-4, differing from NDM-1 …

Biochemical characterization of New Delhi metallo-β-lactamase variants reveals differences in protein stability

A Makena, J Brem, I Pfeffer, REJ Geffen… - Journal of …, 2015 - academic.oup.com
Objectives Metallo-β-lactamase (MBL)-based resistance is a threat to the use of most β-
lactam antibiotics. Multiple variants of the New Delhi MBL (NDM) have recently been …