Choline-phosphate cytidylyltransferase

Summary

Choline-phosphate cytidylyltransferase (EC 2.7.7.15) is an enzyme that catalyzes the chemical reaction

choline-phosphate cytidylyltransferase
Identifiers
EC no.2.7.7.15
CAS no.9026-34-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
CTP + choline phosphate diphosphate + CDP-choline

where the two substrates of this enzyme are CTP and choline phosphate, and the two products are diphosphate and CDP-choline. It is responsible for regulating phosphatidylcholine content in membranes.

This enzyme belongs to the family of transferases, specifically those 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. This enzyme participates in aminophosphonate metabolism and glycerophospholipid metabolism.

Structural studies edit

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1PEH and 1PEI.

References edit

  • BORKENHAGEN LF, KENNEDY EP (1957). "The enzymatic synthesis of cytidine diphosphate choline". J. Biol. Chem. 227 (2): 951–62. PMID 13463016.
  • KENNEDY EP, WEISS SB (1956). "The function of cytidine coenzymes in the biosynthesis of phospholipides". J. Biol. Chem. 222 (1): 193–214. 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. PMID 13376620.