Abstract
The licC gene product of Streptococcus pneumoniae was expressed and characterized. LicC is a nucleoside triphosphate transferase family member and possesses CTP:phosphocholine cytidylyltransferase activity. Phosphoethanolamine is a poor substrate. The LicC protein plays a role in the biosynthesis of the phosphocholine-derivatized cell wall constituents that are critical for cell separation and pathogenesis.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Choline-Phosphate Cytidylyltransferase / chemistry
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Choline-Phosphate Cytidylyltransferase / genetics*
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Choline-Phosphate Cytidylyltransferase / metabolism*
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Chromatography, Affinity
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Gene Amplification
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Kinetics
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Molecular Sequence Data
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Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry
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Phosphoenolpyruvate Sugar Phosphotransferase System / genetics*
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Phosphoenolpyruvate Sugar Phosphotransferase System / metabolism*
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Pseudomonas aeruginosa / enzymology
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Pseudomonas aeruginosa / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
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Streptococcus pneumoniae / enzymology*
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Streptococcus pneumoniae / genetics*
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Substrate Specificity
Substances
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Recombinant Proteins
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Phosphoenolpyruvate Sugar Phosphotransferase System
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cellobiose phosphotransferase B
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Choline-Phosphate Cytidylyltransferase