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.
| 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 |
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Samuelsen, O., Castanheira, M., Walsh, TR., & Spencer, J. (2008). Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family. Antimicrobial Agents and Chemotherapy, 52(8), 2905 - 2908. https://doi.org/10.1128/AAC.00166-08