Biochemical characterization of metallo-beta-lactamase VIM-11 from a Pseudomonas aeruginosa clinical strain.
A detailed biochemical characterization of the Pseudomonas aeruginosa VIM-11 metallo-beta-lactamase (MbetaL) is reported. The only substitution differentiating VIM-11 from VIM-2 (N165S) promoted a slightly improved catalytic efficiency of the former on 3 out of 12 substrates, notably the bulky cephalosporins. Thus, MbetaL-mediated resistance also may be modulated by remote mutations.
Marchiaro
Patricia
P
Departamento de Microbiología, Instituto de Biología Molecular y Celular de Rosario (IBR, CONICET), Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Buenos Aires, Argentina.
Tomatis
Pablo E
PE
Mussi
María A
MA
Pasteran
Fernando
F
Viale
Alejandro M
AM
Limansky
Adriana S
AS
Vila
Alejandro J
AJ
D001665:Binding Sites; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics*; D006801:Humans; D007700:Kinetics; D008826:Microbial Sensitivity Tests; D008958:Models, Molecular; D010957:Plasmids; D011552:Pseudomonas Infections / Q000382:microbiology; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000201:enzymology* / Q000302:isolation & purification; D018440:beta-Lactam Resistance; D001618:beta-Lactamases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D047090:beta-Lactams / Q000378:metabolism / Q000494:pharmacology*
D047090:beta-Lactams; C425108:beta-lactamase bla(vim-2); D001618:beta-Lactamases