Mar 1, 1996

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

The Journal of Antimicrobial Chemotherapy
Timothy R WalshPeter 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.

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Mentioned in this Paper

Bacterial Proteins
beta-Lactams
Aeromonas hydrophila
Enzymes, antithrombotic
Carbapenems
Amino Acids, I.V. solution additive
Cyanophycin Synthetase Activity
Nucleic Acid Sequencing
Homologous Sequences, Amino Acid
CphA protein, Aeromonas hydrophila

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