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Jacquin, O., Balbeur, D., Damblon, C., Marchot, P., De Pauw, E., Roberts, G.C., Frere, J.M. and Matagne, A. (2009) Positively Cooperative Binding of Zinc Ions to Bacillus cereus 569/H/9 β-Lactamase II Suggests that the Binuclear Enzyme Is the Only Relevant Form for Catalysis. Journal of Molecular Biology, 392, 1278-1291.
http://dx.doi.org/10.1016/j.jmb.2009.07.092

has been cited by the following article:

• TITLE: Metallo-β-Lactamases: A Major Threat to Human Health

  AUTHORS: Emer K. Phelan, Manfredi Miraula, Christopher Selleck, David L. Ollis, Gerhard Schenk, Nataša Mitić

  KEYWORDS: Antibiotic Resistance, β-Lactam Antibiotics, Metallo-β-Lactamases, Reaction Mechanism, Metal Ion Binding

  JOURNAL NAME: American Journal of Molecular Biology, Vol.4 No.3, July 16, 2014

  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-memberedβ-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 theβ-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.