Phosphatidylserine decarboxylase
From Wikipedia, the free encyclopedia
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.
[edit] References
- IUBMB entry for 4.1.1.65
- BRENDA references for 4.1.1.65 (Recommended.)
- PubMed references for 4.1.1.65
- PubMed Central references for 4.1.1.65
- Google Scholar references for 4.1.1.65
- 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: 479–83. PMID 338609.
[edit] External links
-
- The CAS registry number for this enzyme class is 9054-78-8.