phosphatidylserine decarboxylase
Identifiers
EC no.4.1.1.65
CAS no.9054-78-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Phosphatidylserine decarboxylase
Identifiers
SymbolPSD
PfamPF02666
InterProIPR003817
Membranome595
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure 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.


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