Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial matrix | - |
Arabidopsis thaliana | 5759 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Arabidopsis thaliana |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [pyruvate dehydrogenase (acetyl-transferring)] | Arabidopsis thaliana | phosphorylation at Ser292 by PDK1 | ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [pyruvate dehydrogenase (acetyl-transferring)] | phosphorylation at Ser292 by PDK1 | Arabidopsis thaliana | ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate | - |
r | |
ATP + [pyruvate dehydrogenase (acetyl-transferring)] | reversible phosphorylation of alpha2beta2-heterotetrameric pyruvate dehydrogenase complex, i.e. E1, phosphorylation at Ser292 within the active-site loop structure of E1alpha by PDK1. Substrate mutation of Asp295 to Ala, Asn, or Leu greatly reduces phosphorylation of Ser292, while mutation of Gly297 has relatively little effect. AtPDC E1alpha S298A mutant is phosphorylated by AtPDK. Activity of the enzyme with different substrate mutants, overview | Arabidopsis thaliana | ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate | - |
r | |
additional information | pyruvate dehydrogenase Asp295 plays an important role in stabilizing the active-site loop structure of the pyruvate dehydrogenase, facilitating transfer of the gamma-phosphate from ATP to the Ser residue at regulatory site one of E1alpha, substrate structure, overview | Arabidopsis thaliana | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
E1-kinase | - |
Arabidopsis thaliana |
PDK | - |
Arabidopsis thaliana |
pyruvate dehydrogenase-kinase | - |
Arabidopsis thaliana |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Arabidopsis thaliana |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Arabidopsis thaliana |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Arabidopsis thaliana |