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Literature summary extracted from

  • Satre, M.; Kennedy, E.P.
    Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli (1978), J. Biol. Chem., 253, 479-483.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.65 4-Bromo-3-hydroxybenzyloxyamine
-
 Escherichia coli
4.1.1.65 Cyanoborohydride inactivation in presence of phosphatidylserine, no inactivation in absence of phosphatidylserine Escherichia coli
4.1.1.65 Hydrazines phenylhydrazine Escherichia coli
4.1.1.65 hydroxylamine
-
 Escherichia coli
4.1.1.65 O-Benzylhydroxylamine
-
 Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.1.1.65 membrane intrinsic membrane protein Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.65 phosphatidyl-L-serine Escherichia coli the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.65 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.1.65 phosphatidyl-L-serine = phosphatidylethanolamine + CO2 a Schiff base is formed by addition of the amino group of phosphatidylserine to the pyruvate residue of the enzyme as an essential step in the action of the decarboxylase Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.65 Phosphatidyl-L-serine
-
 Escherichia coli Phosphatidylethanolamine + CO2
-
 ?
4.1.1.65 phosphatidyl-L-serine the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine Escherichia coli ?
-
 ?