Phosphatidylserine decarboxylase

phosphatidylserine decarboxylase
Identifiers
EC number 4.1.1.65
CAS number 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 / EGO

In enzymology, a phosphatidylserine decarboxylase (EC 4.1.1.65) is an enzyme that catalyzes the chemical reaction

phosphatidyl-L-serine \rightleftharpoons 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: 17206. 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): 47983. PMID 338609. 
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