Phosphatidylserine decarboxylase

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phosphatidylserine decarboxylase
Identifiers
EC number4.1.1.65
CAS number9054-78-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Phosphatidylserine decarboxylase
Identifiers
SymbolPSD
PfamPF02666
InterProIPR003817
Membranome595

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[edit]

  • 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.