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.
Samuelsen
Ørjan
Ø
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
Castanheira
Mariana
M
Walsh
Timothy R
TR
Spencer
James
J
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