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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Saccharomyces cerevisiae |
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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + Cdc28-cyclin B | - |
Saccharomyces cerevisiae | ADP + phospho-Cdc28-cyclin B | - |
? | |
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 | - |
? | |
ATP + Pho85-Pho80 | - |
Saccharomyces cerevisiae | ADP + phospho-Pho85-Pho80 | - |
? | |
ATP + protein kinase A | - |
Saccharomyces cerevisiae | ADP + phospho-protein kinase A | - |
? | |
ATP + protein kinase C | - |
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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
casein kinase II | - |
Saccharomyces cerevisiae |
CKII | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Saccharomyces cerevisiae |
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 |