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|
|Pages (from-to)||2905 - 2908|
|Number of pages||4|
|Journal||Antimicrobial Agents and Chemotherapy|
|Publication status||Published - Aug 2008|