Organism | UniProt | Comment | Textmining |
---|---|---|---|
Dromiciops gliroides | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | component E1 is subject to regulation by phosphorylation at residues S232, S293, S300 | Dromiciops gliroides |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
heart | - |
Dromiciops gliroides | - |
kidney | - |
Dromiciops gliroides | - |
liver | - |
Dromiciops gliroides | - |
skeletal muscle | - |
Dromiciops gliroides | - |
General Information | Comment | Organism |
---|---|---|
physiological function | within the complex, the E1 enzyme pyruvate dehydrogenase (PDH) is the main regulatory site and is subject to inhibitory phosphorylation. Total PDH content does not change significantly during hibernation in any tissue but phospho-PDH content increases in all. Heart PDH shows increased phosphorylation at the three sites S232, S293, S300 by 8.1-, 10.6- and 2.1fold, respectively. Liver also shows elevated phospho-S300 (2.5fold) and phospho-S293 (4.7fold) content. Phosphorylation of S232 and S293 increases significantly in brain and lung but only S232 phosphorylation increases in kidney and skeletal muscle | Dromiciops gliroides |