Abstract
The interaction between tazobactam and several chromosome- and plasmid-encoded (TEM, SHV, PSE types) class A and C beta-lactamases was studied by spectrophotometry. Tazobactam behaved as a competitive inhibitor or inactivator able to restore in several cases the efficiency of piperacillin as a partner beta-lactam. A detailed kinetic analysis permitted measurement of the acylation efficiency for some cephalosporinases and broad-spectrum beta-lactamases; the presence of a turn-over of acyl-enzyme complex was also evaluated.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acinetobacter / drug effects
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Acinetobacter / enzymology
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Binding Sites
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Citrobacter / drug effects
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Citrobacter / enzymology
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Enzyme Inhibitors / pharmacokinetics
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Enzyme Inhibitors / pharmacology
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Escherichia coli / drug effects
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Escherichia coli / enzymology
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Kinetics
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Klebsiella pneumoniae / drug effects
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Klebsiella pneumoniae / enzymology
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Microbial Sensitivity Tests
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Morganella / drug effects
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Morganella / enzymology
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Mycobacterium fortuitum / drug effects
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Mycobacterium fortuitum / enzymology
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Penicillanic Acid / analogs & derivatives*
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Penicillanic Acid / pharmacokinetics
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Penicillanic Acid / pharmacology
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Providencia / drug effects
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Providencia / enzymology
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Pseudomonas aeruginosa / drug effects
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Pseudomonas aeruginosa / enzymology
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Serine*
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Serratia marcescens / drug effects
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Serratia marcescens / enzymology
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Tazobactam
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beta-Lactamase Inhibitors*
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beta-Lactamases / chemistry*
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beta-Lactamases / genetics
Substances
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Enzyme Inhibitors
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beta-Lactamase Inhibitors
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Serine
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Penicillanic Acid
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beta-Lactamases
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Tazobactam