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Details on Person Activated PKA (protein kinase A) phosphorylates serine 36 of...
| Class:Id | Summation:164143 |
|---|---|
| _displayName | Activated PKA (protein kinase A) phosphorylates serine 36 of... |
| _timestamp | 2024-01-08 19:57:24 |
| created | [InstanceEdit:164169] Gopinathrao, G, 2005-05-11 18:49:22 |
| literatureReference | [LiteratureReference:164057] Regulation of fructose-6-phosphate 2-kinase by phosphorylation and dephosphorylation: possible mechanism for coordinated control of glycolysis and glycogenolysis |
| modified | [InstanceEdit:164203] Gopinathrao, G, 2005-05-12 21:32:40 [InstanceEdit:164336] Gopinathrao, G, 2005-05-18 22:14:39 [InstanceEdit:165156] Gopinathrao, G, 2005-07-29 21:00:28 [InstanceEdit:617378] D'Eustachio, P, 2010-04-21 [InstanceEdit:9857755] D'Eustachio, Peter, 2024-01-08 |
| text | Activated PKA (protein kinase A) phosphorylates serine 36 of the bifunctional 6-Phosphofructo-2-kinase /Fructose-2,6-bisphosphatase (PFKFB1) enzyme. This phosphorylation inhibits the enzyme's phosphofructokinase (PFK-2) activity while activating its phosphatase activity. As a result, cytosolic levels of Fructose-2,6-bisphosphate (F-2,6-P2) are reduced. F-2,6-P2 in turn is a key positive regulator of the committed step of glycolysis, so the net effect of this phosphorylation event is a reduced rate of glycolysis. |
| (summation) | [Reaction:163773] PKA tetramer:cAMP phosphorylates PF2K-Pase [Homo sapiens] |
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