Kinetic Characterization of VIM-7, a Divergent Member of the VIM Metallo-β-Lactamase Family

Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family.

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.

VIM-1 Metallo-β-lactamase in Acinetobacter baumannii

In 2004 and 2005, 5 metallo-beta-lactamase (MBL)-positive Acinetobacter baumannii isolates were found in 2 Greek hospitals. Isolates were unrelated and carried blaVIM-1 in a class 1 integron; bla(OXA-51-) and bla(OXA-58-like) carbapenemase genes were also detected. VIM-1 MBL in Acinetobacter spp. causes concern, given the increasing resistance of this species.

Identification of the first VIM metallo - β - lactamase producing multiresistant Aeromonas 1 hydrophila strain 2 3 Running title : VIM metallo - β - lactamase producing A . hydrophila 4 5

VIM-47, a New Variant of the Autochthonous Metallo-β-Lactamase VIM-13 from the Balearic Islands in Spain.

Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-β-lactamase VIM-2

This study examines metal binding to metallo-β-lactamase VIM-2, demonstrating the first successful preparation of a Co(II)-substituted VIM-2 analogue. Spectroscopic studies of the half- and fully metal loaded enzymes show that both Zn(II) and Co(II) bind cooperatively, where the major species present, regardless of stoichiometry, are apo- and di-Zn (or di-Co) enzymes. We determined the di-Zn VI...