Abstract
Purified recombinant VIM-7 possesses efficient penicillinase and carbapenemase activities comparable to those of VIM-2. Cephalosporinase activity was variable and generally lower than those of VIM-1 and VIM-2. A homology model suggests that the VIM-7 Tyr-218 Phe substitution may be responsible for the reduced catalytic efficiency against certain cephalosporins, including ceftazidime and cefepime.
Translated title of the contribution | Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family |
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Original language | English |
Pages (from-to) | 2905 - 2908 |
Number of pages | 4 |
Journal | Antimicrobial Agents and Chemotherapy |
Volume | 52 |
Issue number | 8 |
DOIs | |
Publication status | Published - Aug 2008 |