EC 2.7.7.39 - Glycerol-3-phosphate cytidylyltransferase

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IntEnz Enzyme Nomenclature
EC 2.7.7.39

Names

Accepted name:
glycerol-3-phosphate cytidylyltransferase
Other names:
CDP-glycerol pyrophosphorylase
CTP:glycerol 3-phosphate cytidylyltransferase
Gro-PCT
cytidine diphosphate glycerol pyrophosphorylase
cytidine diphosphoglycerol pyrophosphorylase
CDP-glycerol diphosphorylase
tagD (gene name)
tarD (gene name)
Systematic name:
CTP:sn-glycerol-3-phosphate cytidylyltransferase

Reaction

Comments:

Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047348
CAS Registry Number: 9027-11-6
UniProtKB/Swiss-Prot:

References

  1. Shaw, D.R.D.
    Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol.
    Biochem. J. 82 : 297-312 (1962).
  2. Park, Y. S., Sweitzer, T. D., Dixon, J. E., Kent, C.
    Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis.
    J. Biol. Chem. 268 : 16648-16654 (1993). [PMID: 8393871]
  3. Sanker, S., Campbell, H. A., Kent, C.
    Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase.
    J. Biol. Chem. 276 : 37922-37928 (2001). [PMID: 11487587]
  4. Badurina, D. S., Zolli-Juran, M., Brown, E. D.
    CTP:glycerol 3-phosphate cytidylyltransferase (TarD) from Staphylococcus aureus catalyzes the cytidylyl transfer via an ordered Bi-Bi reaction mechanism with micromolar K(m) values.
    Biochim. Biophys. Acta 1646 : 196-206 (2003). [PMID: 12637027]
  5. Pattridge, K. A., Weber, C. H., Friesen, J. A., Sanker, S., Kent, C., Ludwig, M. L.
    Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis.
    J. Biol. Chem. 278 : 51863-51871 (2003). [PMID: 14506262]

[EC 2.7.7.39 created 1972]