Glycerol-3-phosphate cytidylyltransferase
| Glycerol-3-phosphate cytidylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.39 | ||||||||
| CAS no. | 9027-11-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39) is an enzyme that catalyzes the reversible chemical reaction
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-CDP-glycerol.svg.png)
The enzyme characterised from Lactobacillus arabinosus and Bacillus subtilis combines cytidine triphosphate and (R)-glycerol 1-phosphate to give (2R)-CDP-glycerol, with pyrophosphate (PPi) as a byproduct.[1][2] The mechanism of reaction in Staphylococcus aureus has been studied and is a part of the biosynthesis of teichoic acid.[3][4][5]
This enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:sn-glycerol-3-phosphate cytidylyltransferase. Other names in common use include CDP-glycerol pyrophosphorylase, cytidine diphosphoglycerol pyrophosphorylase, cytidine diphosphate glycerol pyrophosphorylase, CTP:glycerol 3-phosphate cytidylyltransferase, and Gro-PCT.[6]
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1COZ, PDB: 1N1D, and PDB: 2B7L.
References
- ↑ Shaw, DRD (1962). "Pyrophosphorolysis and enzymic synthesis of cytidine diphosphate glycerol and cytidine diphosphate ribitol". Biochemical Journal. 82 (2): 297–312. doi:10.1042/bj0820297. PMC 1243453. PMID 13911452.
- ↑ Park, Y.S.; Sweitzer, T.D.; Dixon, J.E.; Kent, C. (1993). "Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis". Journal of Biological Chemistry. 268 (22): 16648–16654. doi:10.1016/S0021-9258(19)85467-4. PMID 8393871.
- ↑ Sanker, Subramaniam; Campbell, Heidi A.; Kent, Claudia (2001). "Negative Cooperativity of Substrate Binding but Not Enzyme Activity in Wild-type and Mutant Forms of CTP:Glycerol-3-Phosphate Cytidylyltransferase". Journal of Biological Chemistry. 276 (41): 37922–37928. doi:10.1074/jbc.M107198200. PMID 11487587.
- ↑ Badurina, David S.; Zolli-Juran, Michela; Brown, Eric D. (2003). "CTP:glycerol 3-phosphate cytidylyltransferase (TarD) from Staphylococcus aureus catalyzes the cytidylyl transfer via an ordered Bi–Bi reaction mechanism with micromolar Km values". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1646 (1–2): 196–206. doi:10.1016/S1570-9639(03)00019-0. PMID 12637027.
- ↑ Pattridge, Katherine A.; Weber, Christian H.; Friesen, Jon A.; Sanker, Subramaniam; Kent, Claudia; Ludwig, Martha L. (2003). "Glycerol-3-phosphate Cytidylyltransferase". Journal of Biological Chemistry. 278 (51): 51863–51871. doi:10.1074/jbc.M306174200. PMID 14506262.
- ↑ Enzyme 2.7.7.39 at KEGG Pathway Database.