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Literature summary for 2.7.11.1 extracted from

  • Hsieh, L.; Su, W.; Han, G.; Carman, G.
    Phosphorylation of yeast Pah1 phosphatidate phosphatase by casein kinase II regulates its function in lipid metabolism (2016), J. Biol. Chem., 291, 9974-9990.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00023
-
Pah1 phosphatidate phosphatase at pH 7.5 and 30°C Saccharomyces cerevisiae
0.0055
-
ATP at pH 7.5 and 30°C Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + Pah1 phosphatidate phosphatase Saccharomyces cerevisiae more than 90% of its phosphorylation occurs on Thr-170, Ser-250, Ser-313, Ser-705, Ser-814, and Ser-818 ADP + phosphorylated Pah1 phosphatidate phosphatase
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
IgG-Sepharose affinity column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Pah1 phosphatidate phosphatase more than 90% of its phosphorylation occurs on Thr-170, Ser-250, Ser-313, Ser-705, Ser-814, and Ser-818 Saccharomyces cerevisiae ADP + phosphorylated Pah1 phosphatidate phosphatase
-
?

Synonyms

Synonyms Comment Organism
casein kinase II
-
Saccharomyces cerevisiae
CKII
-
Saccharomyces cerevisiae