Phosphatidylserine decarboxylase
| phosphatidylserine decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.65 | ||||||||
| CAS no. | 9054-78-8 | ||||||||
| 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 phosphatidylserine decarboxylase (EC 4.1.1.65) is an enzyme that catalyzes the chemical reaction
- phosphatidyl-L-serine phosphatidylethanolamine + CO2
Hence, this enzyme has one substrate, phosphatidyl-L-serine, and two products, phosphatidylethanolamine and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is phosphatidyl-L-serine carboxy-lyase (phosphatidylethanolamine-forming). Other names in common use include PS decarboxylase, and phosphatidyl-L-serine carboxy-lyase. This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism. It has 2 cofactors: pyridoxal phosphate, and Pyruvate.
References
- KANFER J, KENNEDY EP (1964). "METABOLISM AND FUNCTION OF BACTERIAL LIPIDS. II. BIOSYNTHESIS OF PHOSPHOLIPIDS IN ESCHERICHIA COLI". J. Biol. Chem. 239: 1720–6. PMID 14213340.
- Satre M, Kennedy EP (1978). "Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli". J. Biol. Chem. 253 (2): 479–83. PMID 338609.