| EC Tree |
| 2. Transferases |
| 2.7 Transferring phosphorus-containing groups |
| 2.7.7 Nucleotidyltransferases |
| ID: | 2.7.7.15 |
|---|---|
| Description: | Choline-phosphate cytidylyltransferase. |
| Alternative Name: |
Phosphorylcholine transferase. CTP:phosphocholine cytidylyltransferase. |
| Cath: | 3.40.50.620; 3.90.550.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.7.7.15 |
| BRENDA Enzyme Link: | BRENDA 2.7.7.15 |
| KEGG Enzyme Link: | KEGG2.7.7.15 |
| BioCyc Enzyme Link: | BioCyc 2.7.7.15 |
| ExPASy Enzyme Link: | ExPASy2.7.7.15 |
| EC2PDB Enzyme Link: | EC2PDB 2.7.7.15 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.7.7.15 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.7.7.15 |
| IntEnz Enzyme Link: | IntEnz 2.7.7.15 |
| MEDLINE Enzyme Link: | MEDLINE 2.7.7.15 |
| RHEA:18997 | CTP + H(+) + phosphocholine = CDP-choline + diphosphate |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:7]-[*:8].[H+;H0:9]>>[*:8]-[OH;+0:7].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:2]-[*:1] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The role of histidine residues in the HXGH site of CTP:phosphocholine cytidylyltransferase in CTP binding and catalysis. | Veitch DP, Gilham D, Cornell RB | 1998 Jul 1 | 9692923 |
| Kinetic and biochemical properties of CTP:choline-phosphate cytidylyltransferase from the rat brain. | Mages F, Rey C, Fonlupt P, Pacheco H | 1988 Dec 15 | 2850176 |
| Molecular cloning and characterization of the gene encoding cholinephosphate cytidylyltransferase in Saccharomyces cerevisiae. | Tsukagoshi Y, Nikawa J, Yamashita S | 1987 Dec 15 | 2826147 |
| Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold. | Lee J, Johnson J, Ding Z, Paetzel M, Cornell RB | 2009 Nov 27 | 19783652 |
| Identification of lysine 122 and arginine 196 as important functional residues of rat CTP:phosphocholine cytidylyltransferase alpha. | Helmink BA, Braker JD, Kent C, Friesen JA | 2003 May 6 | 12718547 |