Abstract
The carbapenem-hydrolyzing beta-lactamase SFC-1 from Serratia fonticola UTAD54 was overexpressed in Escherichia coli, purified, and characterized. The enzyme exhibited an apparent molecular mass of 30.5 kDa, determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. SFC-1 hydrolyzes penicillins, cephalosporins, aztreonam, and carbapenems and is inhibited by clavulanic acid, sulbactam, and tazobactam.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aztreonam / metabolism
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Carbapenems / metabolism*
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Catalysis / drug effects
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Cephalosporins / metabolism
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Clavulanic Acid / pharmacology
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics
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Hydrolysis / drug effects
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Kinetics
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Molecular Weight
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Penicillanic Acid / analogs & derivatives
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Penicillanic Acid / pharmacology
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Penicillins / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Serratia / enzymology*
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Serratia / genetics
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Sulbactam / pharmacology
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Tazobactam
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beta-Lactamases / chemistry
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beta-Lactamases / genetics
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beta-Lactamases / metabolism*
Substances
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Carbapenems
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Cephalosporins
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Penicillins
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Recombinant Proteins
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Clavulanic Acid
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Penicillanic Acid
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beta-Lactamases
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Aztreonam
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Sulbactam
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Tazobactam