Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a.
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.
Walsh
T R
TR
Department of Microbiology and Pathology, School of Medical Sciences, University of Bristol, UK.
Gamblin
S
S
Emery
D C
DC
MacGowan
A P
AP
Bennett
P M
PM
D000333:Aeromonas / Q000201:enzymology*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D007700:Kinetics; D008027:Light; D008969:Molecular Sequence Data; D012542:Scattering, Radiation; D017386:Sequence Homology, Amino Acid; D015032:Zinc / Q000378:metabolism; D001618:beta-Lactamases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism*
D001426:Bacterial Proteins; D004492:Edetic Acid; D001618:beta-Lactamases; D015032:Zinc