Function of phosphorylation sites on pyruvate dehydrogenase
| Autor: | Stephen J. Yeaman, Flora H. Pettit, W. Martin Teague, Lester J. Reed |
|---|---|
| Rok vydání: | 1979 |
| Předmět: |
Pyruvate decarboxylation
Pyruvate dehydrogenase lipoamide kinase isozyme 1 Binding Sites Pyruvate dehydrogenase kinase Chemistry Phosphatase Biophysics Pyruvate Dehydrogenase Complex Cell Biology Pyruvate dehydrogenase phosphatase Kidney Pyruvate dehydrogenase complex Biochemistry Molecular biology Dephosphorylation Kinetics Animals Phosphorylation Cattle Molecular Biology |
| Zdroj: | Biochemical and Biophysical Research Communications. 87:244-252 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(79)91672-3 |
| Popis: | Evidence is presented that dephosphorylation of the three phosphorylation sites on bovine kidney pyruvate dehydrogenase by pyruvate dehydrogenase phosphatase is random. The relative rates of dephosphorylation were in the order site 2 > site 3 > site 1. Phosphorylation site 2, and possibly site 3, function, in addition to site 1, as inactivating sites. However, the presence of phosphoryl groups at sites 2 and 3 did not significantly affect the rate of dephosphorylation at site 1 or the rate of reactivation of the enzyme by the phosphatase. The rate-limiting step in the reactivation of phosphorylated pyruvate dehydrogenase is apparently the dephosphorylation at site 1. |
| Databáze: | OpenAIRE |
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