Metallo-β-lactamases: a major threat to human health

Phelan, Emer K., Miraula, Manfred, Selleck, Christopher, Ollis, David L., Schenk, Gerhard and Mitic, Natasa (2014) Metallo-β-lactamases: a major threat to human health. American Journal of Molecular Biology, 4 3: 89-104. doi:10.4236/ajmb.2014.43011

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Author Phelan, Emer K.
Miraula, Manfred
Selleck, Christopher
Ollis, David L.
Schenk, Gerhard
Mitic, Natasa
Title Metallo-β-lactamases: a major threat to human health
Journal name American Journal of Molecular Biology   Check publisher's open access policy
ISSN 2161-6620
Publication date 2014-07-01
Year available 2014
Sub-type Critical review of research, literature review, critical commentary
DOI 10.4236/ajmb.2014.43011
Open Access Status DOI
Volume 4
Issue 3
Start page 89
End page 104
Total pages 16
Place of publication Irvine, CA United States
Publisher Scientific Research Publishing, Inc.
Collection year 2015
Language eng
Formatted abstract
Antibiotic resistance is one of the most significant challenges facing global healthcare. Since the 1940s, antibiotics have been used to fight infections, initially with penicillin and subsequently with various derivatives including cephalosporins, carbapenams and monobactams. A common characteristic of these antibiotics is the four-membered β-lactam ring. Alarmingly, in recent years an increasing number of bacteria have become resistant to these antibiotics. A major strategy employed by these pathogens is to use Zn(II)-dependent enzymes, the metallo-β-lactamases (MBLs), which hydrolyse the β-lactam ring. Clinically useful MBL inhibitors are not yet available. Consequently, MBLs remain a major threat to human health. In this review biochemical properties of MBLs are discussed, focusing in particular on the interactions between the enzymes and the functionally essential metal ions. The precise role(s) of these metal ions is still debated and may differ between different MBLs. However, since they are required for catalysis, their binding site may present an alternative target for inhibitor design.
Keyword Antibiotic Resistance
β Lactam Antibiotics
Reaction mechanism
Metal ion binding
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
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Created: Thu, 07 Aug 2014, 13:32:42 EST by Associate Professor Gary Schenk on behalf of School of Chemistry & Molecular Biosciences