Abstract
Cps2L, a thymidylytransferase, is the first enzyme in Streptococcus pneumoniae L-rhamnose biosynthesis and an antibacterial target. We herein report the evaluation of six sugar phosphate analogues selected to further probe Cps2L substrate tolerance. A modified continuous spectrophotometric assay was employed for facile detection of pyrophosphate (PPi) released from nucleotidylyltransfase-catalysed condensation of sugar 1-phosphates and nucleoside triphosphates to produce sugar nucleotides. Additionally, experiments using waterLOGSY NMR spectroscopy were investigated as a complimentary method to evaluate binding affinity to Cps2L.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / chemical synthesis
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Anti-Bacterial Agents / chemistry*
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Bacterial Proteins / antagonists & inhibitors
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Bacterial Proteins / chemistry*
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Diphosphates / analysis
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Enzyme Assays
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry*
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Glucosephosphates / chemistry*
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Kinetics
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Nucleotidyltransferases / antagonists & inhibitors
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Nucleotidyltransferases / chemistry*
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Recombinant Proteins / chemistry
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Spectrophotometry
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Streptococcus pneumoniae / chemistry
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Streptococcus pneumoniae / enzymology
Substances
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Anti-Bacterial Agents
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Bacterial Proteins
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Diphosphates
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Enzyme Inhibitors
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Glucosephosphates
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Recombinant Proteins
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diphosphoric acid
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glucose-1-phosphate
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Nucleotidyltransferases
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glucose-1-phosphate thymidylyltransferase