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Literature summary for 4.1.1.65 extracted from

  • Warner, T.G.; Dennis, E.A.
    Phosphatidylserine decarboxylase: analysis of its action towards unsaturated and saturated phosphatidylserine and the effect of Triton X-100 on activity (1975), Arch. Biochem. Biophys., 167, 761-768.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Triton X-100 effect is related to the molar ratio of triton to phospholipid Tetrahymena pyriformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
phosphatidylserine natural Tetrahymena pyriformis
1.5
-
phosphatidylserine saturated Tetrahymena pyriformis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Tetrahymena pyriformis 16020
-

Organism

Organism UniProt Comment Textmining
Tetrahymena pyriformis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Phosphatidyl-L-serine activity towards natural phosphatidylserine is greater than towards saturated phosphatidylserine Tetrahymena pyriformis Phosphatidylethanolamine + CO2
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
22
-
stable in presence of phosphatidylserine, 75% loss of activity in presence of Triton without phosphatidylserine present Tetrahymena pyriformis