VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates. © 2015 American Society for Microbiology. All Rights Reserved.
Papagiannitsis, C.C., Pollini, S., DE LUCA, F., Rossolini, G.M., Docquier, J.D., Hrabák, J. (2015). Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece. ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 59(12), 7811-7814 [10.1128/AAC.01935-15].
Biochemical Characterization of VIM-39, a VIM-1-Like Metallo-β-Lactamase Variant from a Multidrug-Resistant Klebsiella pneumoniae Isolate from Greece
POLLINI, SIMONA;DE LUCA, FILOMENA;ROSSOLINI, GIAN MARIA;DOCQUIER, JEAN DENIS;
2015-01-01
Abstract
VIM-39, a VIM-1-like metallo-β-lactamase variant (VIM-1 Thr33Ala His224Leu) was identified in a clinical isolate of Klebsiella pneumoniae belonging to sequence type 147. VIM-39 hydrolyzed ampicillin, cephalothin, and imipenem more efficiently than did VIM-1 and VIM-26 (a VIM-1 variant with the His224Leu substitution) because of higher turnover rates. © 2015 American Society for Microbiology. All Rights Reserved.
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https://hdl.handle.net/11365/982017