AMP-activated protein kinase (AMPK) is a heterodimeric protein serine/threonine kinase that is composed of α- (catalytic) and β/γ- (regulatory) subunits. AMPK acts as a sensor of the energy status of cells and ensures survival at times of metabolic stress. AMPK phosphorylates many metabolic enzymes to stimulate catabolic pathways, such as ketogenesis, and inhibit anabolic pathways, such as protein synthesis. The long-term activation of AMPK increases the capacity of cells to produce ATP.
AMPK is regulated by phosphorylation at the Thr-172 residue of the α-subunit by AMPKK and by phosphorylation by calmodulin-dependent protein kinase kinase-β (CamKKβ). In addition, the ratio of AMP:ATP mediates allosteric activation of the enzyme. AMPK is found throughout the body with high concentrations in metabolically active tissues such as the skeletal muscles and liver.
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Literature for AMPK
A collection of over 400 products for kinase research, the listing includes inhibitors of:
- Receptor Tyrosine Kinases
- Protein Kinases A, C, D and G
- PI-3 Kinase, Akt and mTOR
- MAPK Signaling
- Receptor Serine/Threonine Kinases
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April 22 - 26, 2017
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