Abstract
SHV-28, an extended spectrum beta-lactamase from a clinical isolate of Klebsiella pneumoniae , had an isoelectric point of 7.6 and a substrate profile showing preferential hydrolysis for cefotaxime over ceftazidime. It differed from SHV-1 by one amino acid substitution. The conserved S-T-F-K and K-T-G motifs were identified by SHV-28 protein sequencing.
MeSH terms
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Aged
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Amino Acid Sequence
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Amino Acid Substitution / genetics
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Bacterial Proteins / biosynthesis*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Base Sequence
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DNA, Bacterial / chemistry
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DNA, Bacterial / genetics
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Humans
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India
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Isoelectric Point
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Klebsiella Infections / microbiology*
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Klebsiella pneumoniae / drug effects
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Klebsiella pneumoniae / enzymology*
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Male
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Sequence Analysis, DNA
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Substrate Specificity
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beta-Lactamases / biosynthesis*
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beta-Lactamases / chemistry
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beta-Lactamases / genetics
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beta-Lactams / metabolism
Substances
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Bacterial Proteins
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DNA, Bacterial
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beta-Lactams
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beta-Lactamases