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.
Reference Centre for Detection of Antimicrobial Resistance, Department of Microbiology and Infection Control, University Hospital of North Norway, 9038 Tromsø, Norway. orjan.samuelsen@unn.no
Ørjan
Ø
Samuelsen
Mariana
M
Castanheira
Timothy R
TR
Walsh
James
J
Spencer
D000164:Acremonium / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D002384:Catalysis; D020134:Catalytic Domain / Q000235:genetics; D000077723:Cefepime; D002442:Ceftazidime / Q000378:metabolism; D002511:Cephalosporins / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D009154:Mutation; D010405:Penicillinase / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D001426:Bacterial Proteins; D002511:Cephalosporins; D011994:Recombinant Proteins; D000077723:Cefepime; D002442:Ceftazidime; D010405:Penicillinase; D001618:beta-Lactamases; C063912:carbapenemase