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   <subfield code="a">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 &amp; Satta, 1991). Light scattering analysis indicates that ImiS is functionally active as a monomer.</subfield>
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