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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 .
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information saturation kinetics with respect to the concentrations of Pah1 and ATP Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + Pah1 Saccharomyces cerevisiae Pah1 is a bona fide substrate of yeast CKII. Enzyme CKII phosphorylates Pah1 on Thr170, Ser250, Ser313, Ser705, Ser814, and Ser818 ADP + phospho-Pah1
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?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Cdc28-cyclin B
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Saccharomyces cerevisiae ADP + phospho-Cdc28-cyclin B
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?
ATP + Pah1 Pah1 is a bona fide substrate of yeast CKII. Enzyme CKII phosphorylates Pah1 on Thr170, Ser250, Ser313, Ser705, Ser814, and Ser818 Saccharomyces cerevisiae ADP + phospho-Pah1
-
?
ATP + Pah1 phosphorylation of Saccharomyces cerevisiae Pah1 phosphatidate phosphatase. CKII catalyzes the incorporation of 2 mol of phosphate per mol of Pah1. Enzyme CKII phosphorylates Pah1 on Thr170, Ser250, Ser313, Ser705, Ser814, and Ser818, phosphopeptide mapping analysis. Recombinant Escherichia coli-expressed wild-type Pah1 Saccharomyces cerevisiae ADP + phospho-Pah1
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?
ATP + Pho85-Pho80
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Saccharomyces cerevisiae ADP + phospho-Pho85-Pho80
-
?
ATP + protein kinase A
-
Saccharomyces cerevisiae ADP + phospho-protein kinase A
-
?
ATP + protein kinase C
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Saccharomyces cerevisiae ADP + phospho-protein kinase C
-
?
additional information identification of Pah1 phosphorylation sites for CKII including mass spectrometry, phosphopeptide mapping, and phosphoamino acid analyses of wild-type and mutant forms of Pah1, CKII phosphorylation site mutations reduce the phosphorylation of Pah1, overview Saccharomyces cerevisiae ?
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?

Synonyms

Synonyms Comment Organism
casein kinase II
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Saccharomyces cerevisiae
CKII
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
metabolism phosphorylation of yeast Pah1 phosphatidate phosphatase by casein kinase II regulates its function in lipid metabolism. The Nem1-Spo7 protein phosphatase complex dephosphorylates Pah1 to facilitate its interaction with the nuclear/endoplasmic reticulum membrane and to stimulate its PAP activity that is attenuated through the phosphorylations by Pho85-Pho80 and Protein kinase A. Pah1 is subject to the proteasome-mediated degradation in the stationary phase of growth. The degradation, which occurs by the 20S proteasome via a ubiquitin-independent mechanism, is regulated by phosphorylation. For example, the phosphorylations of Pah1 by Pho85-Pho80 and protein kinase A prevent it from degradation by the 20S proteasome, whereas its phosphorylation by protein kinase C stimulates the proteasomal degradation Saccharomyces cerevisiae
physiological function phosphorylation of yeast Pah1 phosphatidate phosphatase by casein kinase II regulates its function in lipid metabolism. CKII phosphorylation of Pah1 does not have a significant effect on the Km or cooperativity for phosphatidate but has a small (13%) inhibitory effect on the Vmax of the reaction. The phosphorylation of Pah1 by CKII has no significant effect on its proteasomal degradation Saccharomyces cerevisiae