| Literature DB >> 9182099 |
T R Walsh1, S Gamblin, D C Emery, A P MacGowan, P M Bennett.
Abstract
The metallo-beta-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 beta-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-beta-lactamase from Aeromonas hydrophila (Massidda, Rossolini & Satta, 1991). Light scattering analysis indicates that ImiS is functionally active as a monomer.Entities:
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Year: 1996 PMID： 9182099 DOI： 10.1093/jac/37.3.423
Source DB: PubMed Journal: J Antimicrob Chemother ISSN： 0305-7453 Impact factor: 5.790