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Journal of Antimicrobial Chemotherapy (1996) 37, 423-431
© 1996 The British Society for Antimicrobial Chemotherapy

research-article

Enzyme kinetics and biochemical analysis of ImiS, the metallo-ß-lactamase from Aeromonas sobria 163a

Timothy R. Walsha, Steven Gamblinb, David C. Emeryb, Alasdair P. MacGowanc and Peter M. Bennetta

aDepartment of Microbiology and Pathology, School of Medical Sciences, University of Bristol Bristol BS8 JTD, UK bNational Medical Research Centre The Ridgeway, Millhill, London NW7 1AA, UK cRegional Antimicrobial Reference Laboratory, Southmead Health Services NHS Trust, Bristol BS10 5NB, UK

Received 4 April 1995; returned 21 August 1995; accepted 28 September 1995

The metallo-ß-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 ß-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-ßlactamase from Aeromonas hydrophila (Massidda, Rossolini & Satta, 1991). Light scattering analysis indicates that ImiS is functionally active as a monomer.


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