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- Title
Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a.
- Authors
Walsh, Timothy R.; Gamblin, Steven; Emery, David C.; MacGowan, Alasdair P.; Bennett, Peter M.; Walsh, T R; Gamblin, S; Emery, D C; MacGowan, A P; Bennett, P M
- Abstract
The metallo-β-lactamase from Aeromonas sobria 163a, ImiS, was isolated in a two stage purification procedure using protein affinity columns. Enzyme kinetics show that ImiS hydrolyses the carbapenems but displays poor activity against other β-lactams. ImiS possesses the narrowest spectrum of activity of the Group 3 enzymes that have been analysed. Sequencing of the 40 N-terminal amino acids show this region to be identical to that of the CphA metallo-βlactamase from Aeromonas hydrophila (Massidda, Rossolini & Satta, 1991). Light scattering analysis indicates that ImiS is functionally active as a monomer.
- Publication
Journal of Antimicrobial Chemotherapy (JAC), 1996, Vol 37, Issue 3, p423
- ISSN
0305-7453
- Publication type
journal article
- DOI
10.1093/jac/37.3.423