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

O Samuelsen; M Castanheira; TR Walsh; J Spencer

doi:10.1128/AAC.00166-08

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

O Samuelsen
, M Castanheira
, TR Walsh
, J Spencer

School of Cellular and Molecular Medicine

Research output: Contribution to journal › Article (Academic Journal) › peer-review

31 Citations (Scopus)

Abstract

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.

Translated title of the contribution	Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family
Original language	English
Pages (from-to)	2905 - 2908
Number of pages	4
Journal	Antimicrobial Agents and Chemotherapy
Volume	52
Issue number	8
DOIs	https://doi.org/10.1128/AAC.00166-08
Publication status	Published - Aug 2008

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title = "Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family",

abstract = "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.",

author = "O Samuelsen and M Castanheira and TR Walsh and J Spencer",

year = "2008",

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pages = "2905 -- 2908",

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publisher = "American Society for Microbiology",

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T1 - Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family

AU - Samuelsen, O

AU - Castanheira, M

AU - Walsh, TR

AU - Spencer, J

PY - 2008/8

Y1 - 2008/8

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/48749133267

U2 - 10.1128/AAC.00166-08

DO - 10.1128/AAC.00166-08

M3 - Article (Academic Journal)

C2 - 18559652

SN - 0066-4804

VL - 52

SP - 2905

EP - 2908

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

IS - 8

ER -

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

Abstract

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