Novel metallo β-lactamase mediated by a Shigella flexneri plasmid

Abstract Novel carbapenem-hydrolyzing β-lactamase (newly named MET-1) encoded on a transferable plasmid pMS390 from Shigella flexneri JS19622 was purified. The molecular weight was 28 000 by SDS-PAGE and the isoelectric point was higher than 9.3. This β-lactamase favorably hydrolyzed classical cepha...

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Bibliographic Details
Published in:FEMS microbiology letters 1998-05, Vol.162 (2), p.201-206
Main Authors: O’Hara, Koji, Haruta, Shin, Sawai, Tetsuo, Tsunoda, Mitsuko, Iyobe, Shizuko
Format: Article
Language:English
Subjects:
Antibiotics
Atomic absorption analysis
Atomic absorption spectrophotometry
Carbapenem resistance
Carbapenems
Cephalosporinase
Cephalosporins
Enzymatic activity
Enzymes
Ethylenediaminetetraacetic acids
Gel electrophoresis
Metallo β‐lactamase
Metallography
Microbiology
Molecular weight
Shigella flexneri
Sodium lauryl sulfate
Spectral analysis
Spectrophotometry
Substrates
Zinc
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Summary:Abstract Novel carbapenem-hydrolyzing β-lactamase (newly named MET-1) encoded on a transferable plasmid pMS390 from Shigella flexneri JS19622 was purified. The molecular weight was 28 000 by SDS-PAGE and the isoelectric point was higher than 9.3. This β-lactamase favorably hydrolyzed classical cephalosporins and oxyimino-cephalosporins rather than penicillins and carbapenems, but did not hydrolyze monobactams. The enzymatic activity was inhibited by EDTA, and the enzyme was found to contain two moles of zinc per mole of enzyme protein by means of atomic absorption spectrophotometry. These results indicated that the enzyme is a zinc β-lactamase which differs from known metallo β-lactamases, especially in its cephalosporinase-type substrate profile.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1998.tb12999.x