Choline-phosphate cytidylyltransferase
| choline-phosphate cytidylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.15 | ||||||||
| CAS no. | 9026-34-0 | ||||||||
| 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 | ||||||||
| |||||||||
Choline-phosphate cytidylyltransferase (EC 2.7.7.15) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from guinea pig liver combines cytidine triphosphate and phosphocholine to give citicoline, with pyrophosphate (PPi) as a byproduct. It is responsible for regulating phosphatidylcholine content in membranes.[1][2][3]
In humans, the enzyme protein is encoded by the genes PCYT1A and PCYT1B.[4][5][6] These have been extensively studied.[7][8][9]
This enzyme is a transferase, specifically one transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:choline-phosphate cytidylyltransferase. Other names in common use include phosphorylcholine transferase, CDP-choline pyrophosphorylase, CDP-choline synthetase, choline phosphate cytidylyltransferase, CTP-phosphocholine cytidylyltransferase, CTP:phosphorylcholine cytidylyltransferase, cytidine diphosphocholine pyrophosphorylase, phosphocholine cytidylyltransferase, phosphorylcholine cytidylyltransferase, and phosphorylcholine:CTP cytidylyltransferase.[10]
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes PDB: 1PEH and PDB: 1PEI.
References
- ↑ Kennedy EP, Weiss SB (1956). "The function of cytidine coenzymes in the biosynthesis of phospholipides". J. Biol. Chem. 222 (1): 193–214. doi:10.1016/S0021-9258(19)50785-2. PMID 13366993.
- ↑ Williams-Ashman HG, Banks J (1956). "Participation of cytidine coenzymes in the metabolism of choline by seminal vesicles". J. Biol. Chem. 223 (1): 509–521. doi:10.1016/S0021-9258(18)65160-9. PMID 13376620.
- ↑ Borkenhagen LF, Kennedy EP (1957). "The enzymatic synthesis of cytidine diphosphate choline". J. Biol. Chem. 227 (2): 951–62. doi:10.1016/S0021-9258(18)70774-6. PMID 13463016.
- ↑ Kalmar GB, Kay RJ, LaChance AC, Cornell RB (Nov 1994). "Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase". Biochim Biophys Acta. 1219 (2): 328–34. doi:10.1016/0167-4781(94)90056-6. PMID 7918629.
- ↑ Lykidis A, Murti KG, Jackowski S (Jul 1998). "Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase". J Biol Chem. 273 (22): 14022–9. doi:10.1074/jbc.273.22.14022. PMID 9593753.
- ↑ Lykidis A, Baburina I, Jackowski S (1999). "Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant". J. Biol. Chem. 274 (38): 26992–7001. doi:10.1074/jbc.274.38.26992. PMID 10480912.
- ↑ Lagace TA, Miller JR, Ridgway ND (2002). "Caspase processing and nuclear export of CTP:phosphocholine cytidylyltransferase alpha during farnesol-induced apoptosis". Mol. Cell. Biol. 22 (13): 4851–62. doi:10.1128/MCB.22.13.4851-4862.2002. PMC 133913. PMID 12052891.
- ↑ Xie M, Smith JL, Ding Z, et al. (2004). "Membrane binding modulates the quaternary structure of CTP:phosphocholine cytidylyltransferase". J. Biol. Chem. 279 (27): 28817–25. doi:10.1074/jbc.M403311200. PMID 15069071.
- ↑ Enaw JO, Zhu H, Yang W, et al. (2007). "CHKA and PCYT1A gene polymorphisms, choline intake and spina bifida risk in a California population". BMC Medicine. 4: 36. doi:10.1186/1741-7015-4-36. PMC 1770928. PMID 17184542.
- ↑ Enzyme 2.7.7.15 at KEGG Pathway Database.