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Literature summary for 4.1.1.65 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

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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