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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
Search
PMC articles
PubMed articles
NCBI proteins
Phosphatidylserine decarboxylase
Identifiers
SymbolPSD
Pfam PF02666
InterPro IPR003817
Membranome 595
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The enzyme phosphatidylserine decarboxylase ( EC 4.1.1.65) catalyzes the chemical reaction

phosphatidyl-L-serine phosphatidylethanolamine + 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 two 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.