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Literature summary extracted from

  • Wu, W.I.; Carman, G.M.
    Kinetic analysis of sphingoid base inhibition of yeast phosphatidate phosphatase (2000), Methods Enzymol., 312, 373-380.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.4 phytosphingosine
-
Saccharomyces cerevisiae
3.1.3.4 psychosine
-
Saccharomyces cerevisiae
3.1.3.4 sphinganine
-
Saccharomyces cerevisiae
3.1.3.4 sphingosine
-
Saccharomyces cerevisiae
3.1.3.4 Stearylamine
-
Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.4 membrane two membrane-associated forms, 45000 Da and 104000 Da, of the Mg2+-dependent phosphatidate phosphatase Saccharomyces cerevisiae 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.4 Mg2+ two membrane-associated forms, 45000 Da and 104000 Da, of the Mg2+-dependent phosphatidate phosphatase Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.4 additional information Saccharomyces cerevisiae the enzyme plays an important role in regulating lipid synthesis in Saccharomyces cerevisiae, the enzyme is also involved in cell signaling mechanisms as part of the phospholipase D-phosphatidate phosphatase pathway ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.4 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.4 additional information the enzyme plays an important role in regulating lipid synthesis in Saccharomyces cerevisiae, the enzyme is also involved in cell signaling mechanisms as part of the phospholipase D-phosphatidate phosphatase pathway Saccharomyces cerevisiae ?
-
?
3.1.3.4 phosphatidate + H2O
-
Saccharomyces cerevisiae 1,2-diacyl-sn-glycerol + phosphate
-
?