[1] Fisher, J.F., Meroueh, S.O. and Mobashery, S. (2005) Bacterial resistance to beta-lactam antibiotics: Compelling opportunism, compelling opportunity. Chemical Reviews, 105, 395-424. http://dx.doi.org/10.1021/cr030102i
[2] Walsh, T.R., Toleman, M.A., Poirel, L. and Nordmann, P. (2005) Metallo-beta-lactamases: The quiet before the storm? Clinical Microbiology Reviews, 182, 306-325.
http://dx.doi.org/10.1128/CMR.18.2.306-325.2005
[3] Escobar Perez, J.A., Olarte Escobar, N.M., Castro-Cardozo, B., Valderrama Marquez, I.A., Garzon Aguilar, M.I., Martinez de la Barrera, L., Barrero Barreto, E.R., Marqeuz-Ortiz, R.A., Moncada Guayazan, M.V. and Vanegas Gomez, N. (2013) Outbreak of NDM-1 producing Klebsiella pneumoniae in a neonatal unit in Colombia. Antimicrobial Agents and Chemotherapy, 57, 1957-1960.
[4] Thomas, P.W., Zheng, M., Wu, S.S., Guo, H., Liu, D.L., Xu, D.G. and Fast, W. (2011) Characterization of Purified New Delhi Metallo-beta-lactamase-1. Biochemistry, 5046, 10102-10113. http://dx.doi.org/10.1021/bi201449r
[5] Laraki, N., Franceschini, N., Rossolini, G.M., Santucci, P., Meunier, C., de Pauw, E., Amicosante, G., Frere, J.M. and Galleni, M. (1999) Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-beta-lactamase IMP-1 produced by Escherichia coli. Antimicrobial Agents and Chemotherapy, 434, 902-906.
[6] Carfi, A., Pares, S., Duee, E., Galleni, M., Duez, C., Frere, J. and Dideberg, O. (1995) The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new-type of protein fold. The EMBO Journal, 1420, 4914-4921.
[7] Crowder, M.W., Wang, Z.G., Franklin, S.L., Zovinka, E. P. and Benkovic, S.J. (1996) Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis. Biochemistry, 3537, 12126-12132.
http://dx.doi.org/10.1021/bi960976h
[8] Murphy, T.A., Catto, L.E., Halford, S.E., Hadfield, A.T., Minor, W., Walsh, T.R. and Specer, J. (2006) Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-beta-lactamases. Journal of Molecular Biology, 3573, 890-903.
http://dx.doi.org/10.1016/j.jmb.2006.01.003
[9] 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
[10] Fonseca, F., Bromley, E.H., Saavedra, M.J., Correia, A. and Spencer, J. (2011) Crystal structure of Serratia fonticolaSfh-I: Activation of the nucleophile in mono-zinc metallo-beta-lactamases. Journal of Molecular Biology, 411, 951-959.
http://dx.doi.org/10.1016/j.jmb.2011.06.043
[11] Leiros, H.K., Borra, P.S., Brandsdal, B.O., Edvardsen, K.S.W., Spencer, J., Walsh, T.R. and Samuelsen, O. (2012) Crystal structure of the mobile metallo-beta-lactamase AIM-1 from Pseudomonas aeruginosa: Insights into antibiotic binding and the role of Gln157. Antimicrobial Agents and Chemotherapy, 568, 4341-4353.
http://dx.doi.org/10.1128/AAC.00448-12
[12] Crowder, M.W., Walsh, T.R., Banovic, L., Pettit, M. and Spencer, J. (1998) Overexpression, purification, and characterization of the cloned metallo-beta-lactamase L1 from Stenotrophomonas maltophilia. Antimicrobial Agents and Chemotherapy, 424, 921-926.
[13] Wachino, J., Yoshida, H., Yamane, K., Suzuki, S., Matsui, M., Yamagishi, T., Tsutsui, A., Konda, T., Shibayama, K. and Arakawa, Y. (2011) SMB-1, a novel subclass B3 metallo-beta-lactamase, associated with ISCR1 and a class 1 integron, from a carbapenem-resistant Serratia marcescens clinical isolate. Antimicrobial Agents and Chemotherapy, 55, 5143-5149.
http://dx.doi.org/10.1128/AAC.05045-11
[14] Miraula, M., Brunton, C., Schenk, G. and Mitic, N. (2013) Identification and preliminary characterization of novel B3-type metallo-β-lactamases. American Journal of Molecular Biology, 3, 198-203.
[15] Vella, P., Miraula, M., Phelan, E., Leung, E.W., Ely, F., Ollis, D.L., McGeary, R.P., Schenk, G. and Mitic, N. (2013) Identification and characterization of an unusual metallo-beta-lactamase from Serratia proteamaculans. Journal of Biological Inorganic Chemistry, 18, 855-863.
http://dx.doi.org/10.1007/s00775-013-1035-z
[16] Guindon, S., Dufayard, J.F., Lefort, V., Anisimova, M., Hordijk, W. and Gascuel, O. (2010) New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0. Systematic Biology, 59, 307-321.
http://dx.doi.org/10.1093/sysbio/syq010
[17] Ivy, R.A., Farber, J.M., Pagotto, F. and Wiedmann, M. (2013) International life science institute north America Cronobacter (formerly Enterobacter sakazakii) isolate set. Journal of Food Protection, 76, 40-51.
http://dx.doi.org/10.4315/0362-028X.JFP-11-546
[18] Friedemann, M. (2009) Epidemiology of invasive neonatal Cronobacter (Enterobacter sakazakii) infections. European Journal of Clinical Microbiology & Infectious Diseases, 28, 1297-1304.
http://dx.doi.org/10.1007/s10096-009-0779-4
[19] Dong, Y.J., Bartlam, M., Sun, L., Zhou, Y.F., Zhang, Z. P., Zhang, C.G., Rao, Z. and Zhang, X.E. (2005) Crystal structure of methyl parathion hydrolase from Pseudomonas sp. WBC-3. Journal of Molecular Biology, 353, 655-663. http://dx.doi.org/10.1016/j.jmb.2005.08.057
[20] Cameron, A.D., Ridderstrom, M., Olin, B., and Mannervik, B. (1999) Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure, 7, 1067-1078.
http://dx.doi.org/10.1016/S0969-2126(99)80174-9
[21] Rasia, R.M. and Vila, A.J. (2002) Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-beta-lactamase. Biochemistry, 41, 1853-1860.
http://dx.doi.org/10.1021/bi010933n
[22] Hernandez Valladares, M., Felici, A., Weber, G., Adolph, H.W., Zeppezauer, M., Rossolini, G.M., Amicosante, G., Frere, J.M. and Galleni, M. (1997) Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-beta-lactamase activity and stability. Biochemistry, 36, 11534-11541.
http://dx.doi.org/10.1021/bi971056h