| CDP-diacylglycerol diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.6.1.26 | ||||||||
| CAS no. | 62213-20-1 | ||||||||
| 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 CDP-diacylglycerol diphosphatase (EC 3.6.1.26) is an enzyme that catalyzes the chemical reaction
- CDP-diacylglycerol + H2O CMP + phosphatidate
Thus, the two substrates of this enzyme are CDP-diacylglycerol and H2O, whereas its two products are CMP and phosphatidate.
This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is CDP-diacylglycerol phosphatidylhydrolase. Other names in common use include cytidine diphosphodiacylglycerol pyrophosphatase, and CDP diacylglycerol hydrolase. This enzyme participates in glycerophospholipid metabolism.
Structural studies[edit]
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2POF.
References[edit]
- Raetz CR, Hirschberg CB, Dowhan W, Wickner WT, Kennedy EP (1972). "A membrane-bound pyrophosphatase in Escherichia coli catalyzing the hydrolysis of cytidine diphosphate-diglyceride". J. Biol. Chem. 247 (7): 2245–7. PMID 4335869.
