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.
PMID14213340.
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.
PMID338609.