The Enzyme Database

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EC 2.7.7.39     
Accepted name: glycerol-3-phosphate cytidylyltransferase
Reaction: CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol
Other name(s): CDP-glycerol pyrophosphorylase; cytidine diphosphoglycerol pyrophosphorylase; cytidine diphosphate glycerol pyrophosphorylase; CTP:glycerol 3-phosphate cytidylyltransferase; Gro-PCT; tagD (gene name); tarD (gene name)
Systematic name: CTP:sn-glycerol-3-phosphate cytidylyltransferase
Comments: Involved in the biosynthesis of teichoic acid linkage units in bacterial cell walls.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-11-6
References:
1.  Shaw, D.R.D. Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol. Biochem. J. 82 (1962) 297–312. [PMID: 13911452]
2.  Park, Y.S., Sweitzer, T.D., Dixon, J.E. and Kent, C. Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis. J. Biol. Chem. 268 (1993) 16648–16654. [PMID: 8393871]
3.  Sanker, S., Campbell, H.A. and 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 (2001) 37922–37928. [DOI] [PMID: 11487587]
4.  Badurina, D.S., Zolli-Juran, M. and 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 (2003) 196–206. [DOI] [PMID: 12637027]
5.  Pattridge, K.A., Weber, C.H., Friesen, J.A., Sanker, S., Kent, C. and 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 (2003) 51863–51871. [DOI] [PMID: 14506262]
[EC 2.7.7.39 created 1972]
 
 


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