Title : Novel VIM metallo-beta-lactamase variant from clinical isolates of Enterobacteriaceae from Algeria.

Pub. Date : 2010 Jan

PMID : 19901092






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 This enzyme was inhibited by EDTA and hydrolyzed penicillins, cephalosporins, and carbapenems, as observed for other VIM-type carbapenemases but with greater catalytic efficiency against penicillins than VIM-1. Cephalosporins vimentin Homo sapiens
2 This enzyme was inhibited by EDTA and hydrolyzed penicillins, cephalosporins, and carbapenems, as observed for other VIM-type carbapenemases but with greater catalytic efficiency against penicillins than VIM-1. Cephalosporins vimentin Homo sapiens