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

25 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

Access to Document

10.1128/AAC.00166-08

http://aac.asm.org/content/52/8/2905

Fingerprint Dive into the research topics of 'Kinetic characterization of VIM-7, a divergent member of the VIM metallo-beta-lactamase family'. Together they form a unique fingerprint.

Cite this

@article{811e7b69d64c4455ab32cab5bb9ca537,

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",

month = aug,

doi = "10.1128/AAC.00166-08",

language = "English",

volume = "52",

pages = "2905 -- 2908",

journal = "Antimicrobial Agents and Chemotherapy",

issn = "0066-4804",

publisher = "American Society for Microbiology",

number = "8",

}

TY - JOUR

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 - http://www.scopus.com/inward/record.url?eid=2-s2.0-48749133267&partnerID=8YFLogxK

U2 - 10.1128/AAC.00166-08

DO - 10.1128/AAC.00166-08

M3 - Article (Academic Journal)

C2 - 18559652

VL - 52

SP - 2905

EP - 2908

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

SN - 0066-4804

IS - 8

ER -

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

Abstract

Access to Document

Other files and links

Cite this