The licC Gene of Streptococcus pneumoniae Encodes a CTP:Phosphocholine Cytidylyltransferase
Open Access
- 15 August 2001
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 183 (16) , 4927-4931
- https://doi.org/10.1128/jb.183.16.4927-4931.2001
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.Keywords
This publication has 21 references indexed in Scilit:
- Lipid Activation of CTP:Phosphocholine Cytidylyltransferase α: Characterization and Identification of a Second Activation DomainBiochemistry, 2000
- Bacterial Phosphorylcholine Decreases Susceptibility to the Antimicrobial Peptide LL-37/hCAP18 Expressed in the Upper Respiratory TractInfection and Immunity, 2000
- Pneumococcal licD2 gene is involved in phosphorylcholine metabolismMolecular Microbiology, 1999
- Molecular and Cellular Biology of Pneumococcal InfectionMicrobial Drug Resistance, 1997
- Investigation of a choline phosphate synthesis pathway in Streptococcus pneumoniae: evidence for choline phosphate cytidylyltransferase activityFEMS Microbiology Letters, 1996
- Enoyl-Acyl Carrier Protein Reductase (fabI) Plays a Determinant Role in Completing Cycles of Fatty Acid Elongation in Escherichia coliJournal of Biological Chemistry, 1995
- Teichoic acid and lipoteichoic acid of Streptococcus pneumoniae possess identical chain structuresEuropean Journal of Biochemistry, 1993
- Cloning and expression of rat liver CTP: phosphocholine cytidylyltransferase: an amphipathic protein that controls phosphatidylcholine synthesis.Proceedings of the National Academy of Sciences, 1990
- Molecular cloning and characterization of the gene encoding cholinephosphate cytidylyltransferase in Saccharomyces cerevisiaeEuropean Journal of Biochemistry, 1987
- Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: chanin formation, loss of transformability, and loss of autolysis.Proceedings of the National Academy of Sciences, 1968