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Literature summary for 3.1.3.4 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
Search for more literature for 3.1.3.4

Inhibitors

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
phosphatidate + H2O
-
 Saccharomyces cerevisiae 1,2-diacyl-sn-glycerol + phosphate
-
 ?