| glycerophosphocholine cholinephosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.4.38 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
The enzyme glycerophosphocholine cholinephosphodiesterase (EC 3.1.4.38) is an enzyme that catalyzes the reaction
- sn-glycero-3-phosphocholine + H2O = glycerol + phosphocholine
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name 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): 436–41. doi: 10.1016/0005-2760(75)90111-3. PMID 166661.
| glycerophosphocholine cholinephosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.4.38 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
The enzyme glycerophosphocholine cholinephosphodiesterase (EC 3.1.4.38) is an enzyme that catalyzes the reaction
- sn-glycero-3-phosphocholine + H2O = glycerol + phosphocholine
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name 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): 436–41. doi: 10.1016/0005-2760(75)90111-3. PMID 166661.