Glycerophosphocholine cholinephosphodiesterase
| glycerophosphocholine cholinephosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.4.38 | ||||||||
| CAS number | 60063-78-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a glycerophosphocholine cholinephosphodiesterase (EC 3.1.4.38) is an enzyme that catalyzes the chemical reaction
- sn-glycero-3-phosphocholine + H2O glycerol + choline phosphate
Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are glycerol and choline phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is sn-glycero-3-phosphocholine cholinephosphohydrolase. This enzyme is also called L-3-glycerylphosphinicocholine cholinephosphohydrolase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WRA.
References
- Abra RM, Quinn PJ (1975). "A novel pathway for phosphatidylcholine catabolism in rat brain homogenates". Biochim. Biophys. Acta. 380 (3): 436&ndash, 41. doi:10.1016/0005-2760(75)90111-3. PMID 166661.
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