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Bebrone, C., Delbruck, H., Kupper, M.B., Scholmer, P., Wilmann, C., Frere, J.M., Fischer, R., Galleni, M. and Hoffmann, K.M. (2009) The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site. Antimicrobial Agents and Chemotherapy, 53, 4464-4471.
http://dx.doi.org/10.1128/AAC.00288-09

has been cited by the following article:

• TITLE: Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes

  AUTHORS: Chun-Feng D. Hou, Emer K. Phelan, Manfredi Miraula, David L. Ollis, Gerhard Schenk, Nataša Mitić

  KEYWORDS: Antibiotic Resistance; β-Lactam Antibiotics; Metallo-β-Lactamases; Sequence Homology; Serratia proteamaculans; Cronobacter sakazakii

  JOURNAL NAME: American Journal of Molecular Biology, Vol.4 No.1, January 3, 2014

  ABSTRACT: Metallo-β-lactamases (MBLs) are a family of Zn2+-dependent enzymes that have contributed strongly to the emergence and spread of antibiotic resistance. Novel members as well as variants of existing members of this family are discovered continuously, compounding their threat to global health care. MBLs are divided into three subgroups, i.e. B1, B2 and B3. The recent discovery of an unusual MBL from Serratia proteamaculans (SPR-1) suggests the presence of an additional subgroup, i.e. B4. A database search reveals that SPR-1 has only one homologue from Cronobacter sakazakii, CSA-1.These two MBLs have a unique active site and may employ a mechanism distinct from other MBLs, but reminiscent of some organophosphate-degrading hydrolases.