EC Number   |
General Information |
Reference |
|---|
   2.7.11.27 | evolution |
AMP-activated protein kinase (AMPK) is an evolutionarily conserved serine/threonine protein kinase |
741308 |
| 2.7.11.27 | malfunction |
phosphorylated enzyme AMPK is involved in impaired glucose metabolism, that increases the risk for squamous cell carcinoma of the head and neck (SCCHN) in humans |
741308 |
| 2.7.11.27 | metabolism |
AMPK activation by metformin regulates acetyl-CoA carboxylase (ACC) activity by its phosphorylation. ACC is a rate-controlling enzyme for the synthesis of malonyl-CoA, which plays a critical role in the synthesis of fatty acids and the inhibition of mitochondrial fatty acid oxidation in the liver. the enzyme activator metformin decreases high-fat diet-induced renal injury by regulating the expression of adipokines and the renal AMP-activated protein kinase/acetyl-CoA carboxylase pathway in mice |
-, 740545 |
| 2.7.11.27 | metabolism |
globular adiponectin regulates energy homeostasis through AMP-activated protein kinase-acetyl-CoA carboxylase (AMPK/ACC) pathway, but not the JAK/STAT3 pathway, in the hypothalamus. Adiponectin increases the phosphorylation and activation of AMPK, it increases inactivated acetyl-CoA carboxylase (ACC), which has been phosphorylated by activated AMPK, and subsequently increases expression of agouti-related peptide (AgRP) mRNA. Adiponectin had no effect on signal transducer and activator of transcription (STAT3), overview |
740990 |
| 2.7.11.27 | metabolism |
the reduction of hypothalamic acetyl-CoA carboxylase increases phophoenolpyruvate carboxykinase expression, AMPK phosphorylation, and glucose production in the liver. These effects are observed without modification of hypothalamic AMPK phosphorylation. Fasted rats show greater AMPK phosphorylation levels than fed rats. Reduced AMPK phosphorylation is linked to an increase in acetyl-CoA carboxylase activity and biosynthesis of malonyl-CoA |
-, 741273 |
| 2.7.11.27 | more |
AMPK is activated in response to metabolic stresses, such as hypoxia and ischemia, and the anti-diabetic drug metformin |
741308 |
| 2.7.11.27 | physiological function |
AMP-activated protein kinase (AMPK) regulates glucose and lipid metabolism via the phosphorylation and subsequent inactivation of its downstream target acetyl-CoA carboxylase (ACC). AMPK acts as a cellular fuel sensor by controlling intracellular energy levels to maintain appropriate cell growth rates. Phosphorylation and activation of AMPK stimulates fatty acid oxidation through the phosphorylation and subsequent inhibition of its downstream target acetyl-CoA carboxylase. Phosphorylated acetyl-CoA carboxylase may play a role in tumor progression of squamous cell carcinoma of the head and neck and may help to identify patient subgroups at high risk for poor disease outcome |
741308 |
| 2.7.11.27 | physiological function |
AMP-activated protein kinase (AMPK) represents an energy sensor that responds to hormone and nutrition status in vivo and exerts a regulatory effect in the hypothalamus and multiple peripheral tissues. AMP-activated protein inhibits acetyl-CoA carboxylase (ACC) through phosphorylation |
740990 |
| 2.7.11.27 | physiological function |
AMPK activation by metformin regulates acetyl-CoA carboxylase (ACC) activity by its phosphorylation. AMP-activated protein kinase (AMPK) is involved in the cellular metabolic response to metabolic stress. Metabolic stress, such as impaired ATP production or accelerated ATP consumption activate the AMP-activated protein kinase (AMPK) system, which acts as a sensor of cellular energy metabolism |
-, 740545 |
| 2.7.11.27 | physiological function |
CTRP1 protein, a regulator of fatty acid metabolism, enhances fatty acid oxidation via AMP-activated protein kinase (AMPK) activation and acetyl-CoA carboxylase (ACC) inhibition |
-, 740699 |
