Abstract
TEM-71, a novel extended-spectrum beta-lactamase from a Klebsiella pneumoniae clinical isolate, had an isoelectric point of 6.0 and a substrate profile showing preferential hydrolysis of cefotaxime over ceftazidime. It differed from TEM-1 by two substitutions, Gly238Ser and Glu240Lys, and was under the control of the strong P4 promoter.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Substitution
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Cefotaxime / metabolism
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Ceftazidime / metabolism
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Cephalosporin Resistance / genetics*
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Cephalosporins / metabolism
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Cephalosporins / pharmacology
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DNA, Bacterial / genetics
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Isoelectric Focusing
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Kinetics
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Klebsiella pneumoniae / drug effects
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Klebsiella pneumoniae / enzymology*
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Klebsiella pneumoniae / genetics*
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Plasmids / genetics*
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Reverse Transcriptase Polymerase Chain Reaction
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Substrate Specificity
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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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Cephalosporins
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DNA, Bacterial
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Ceftazidime
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TEM-71 beta-lactamase
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beta-Lactamases
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Cefotaxime