Activating Compound | Comment | Organism | Structure |
---|---|---|---|
5'-AMP | - |
Saccharomyces cerevisiae | |
5'-AMP | the gamma subunit of AMPK contains adenine nucleotide binding sites that facilitate the direct interaction of AMP with the AMPK heterotrimer. AMP regulates the activity of AMPK via the inhibition of AMPK dephosphorylation by protein phosphatases | Homo sapiens | |
5'-AMP | the gamma subunit of AMPK contains adenine nucleotide binding sites that facilitate the direct interaction of AMP with the AMPK heterotrimer. AMP regulates the activity of AMPK via the inhibition of AMPK dephosphorylation by protein phosphatases | Rattus norvegicus | |
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside | i.e. AICAR, the pharmacological compound transported into cells by the adenosine transporter, and then metabolized by the enzyme adenosine kinase into 5-aminoimidazole-4-carboxamide 1-b-D-ribofuranosyl monophosphate, ZMP, an AMP analogue, which then functions like endogenous AMP by binding to the Bateman domains of AMPK and promoting allosteric activation of the kinase, AICAR does not alter endogenous levels of AMP or ATP, ZMP might prevent the dephosphorylation of AMPK by inhibition of AMP-sensitive phosphatases | Homo sapiens | |
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside | i.e. AICAR, the pharmacological compound transported into cells by the adenosine transporter, and then metabolized by the enzyme adenosine kinase into 5-aminoimidazole-4-carboxamide 1-b-D-ribofuranosyl monophosphate, ZMP, an AMP analogue, which then functions like endogenous AMP by binding to the Bateman domains of AMPK and promoting allosteric activation of the kinase, AICAR does not alter endogenous levels of AMP or ATP, ZMP might prevent the dephosphorylation of AMPK by inhibition of AMP-sensitive phosphatase | Rattus norvegicus | |
A-769662 | activates the liver enzyme, binds to the enzyme, acts allosterically | Rattus norvegicus | |
Ca2+/calmodulin-dependent protein kinase kinase | i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview | Homo sapiens | |
Ca2+/calmodulin-dependent protein kinase kinase | i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview | Rattus norvegicus | |
dinitrophenol | a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview | Homo sapiens | |
dinitrophenol | a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview | Rattus norvegicus | |
interleukin-6 | activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK | Homo sapiens | |
interleukin-6 | activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK | Rattus norvegicus | |
metformin | i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview | Homo sapiens | |
metformin | i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview | Rattus norvegicus | |
additional information | AMPKalpha needs to be activated by phosphorylation on Thr172 | Homo sapiens | |
additional information | AMPKalpha needs to be activated by phosphorylation on Thr172. Reactive oxygen species contribute to AMPK activation, mechanism, overview | Rattus norvegicus | |
pioglitazone | i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in humans via activation of AMPK in skeletal muscle | Homo sapiens | |
pioglitazone | i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle | Rattus norvegicus | |
rosiglitazone | i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in humans via activation of AMPK in skeletal muscle | Homo sapiens | |
rosiglitazone | i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle | Rattus norvegicus | |
rotenone | a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview | Homo sapiens | |
rotenone | a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
A-769662 | allosterically regulates AMPK activity | Rattus norvegicus | |
compound C | i.e. 6-[4-(2-piperidin-1-ylethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a cell-permeable pyrrazolopyrimidine compound that can act as a reversible and ATP competitive inhibitor of AMPK | Homo sapiens | |
compound C | i.e. 6-[4-(2-piperidin-1-ylethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a cell-permeable pyrrazolopyrimidine compound that can act as a reversible and ATP competitive inhibitor of AMPK | Rattus norvegicus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | differential localization patterns of AMPKalpha 1 and AMPKalpha2 | Homo sapiens | - |
- |
additional information | differential localization patterns of AMPKalpha 1 and AMPKalpha2 | Rattus norvegicus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview | Homo sapiens | |
Ca2+ | increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview | Rattus norvegicus | |
Mg2+ | - |
Homo sapiens | |
Mg2+ | - |
Rattus norvegicus | |
Mg2+ | - |
Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview | ? | - |
? | |
additional information | Rattus norvegicus | AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview | ? | - |
? | |
additional information | Saccharomyces cerevisiae | AMP-activated protein kinase acts as a regulator in cellular metabolism, biochemical regulation of AMPK by AMP, protein phosphatases, and upstream kinases, e.g. LKB1, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Saccharomyces cerevisiae | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | AMPKalpha needs to be activated by phosphorylation on Thr172 | Homo sapiens |
phosphoprotein | AMPKalpha needs to be activated by phosphorylation on Thr172 | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
epitrochlearis muscle | - |
Rattus norvegicus | - |
liver | - |
Homo sapiens | - |
liver | - |
Rattus norvegicus | - |
skeletal muscle | - |
Homo sapiens | - |
skeletal muscle | - |
Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview | Homo sapiens | ? | - |
? | |
additional information | AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview | Rattus norvegicus | ? | - |
? | |
additional information | AMP-activated protein kinase acts as a regulator in cellular metabolism, biochemical regulation of AMPK by AMP, protein phosphatases, and upstream kinases, e.g. LKB1, overview | Saccharomyces cerevisiae | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | several isoforms for each of the three AMPK subunits, including alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, AMPKalpha subunit possesses a highly conserved, N-terminal catalytic domain that contains the activating phosphorylation site Thr172, an autoinhibitory domain, and a C-terminus that contains the domains required for binding with the beta and gamma subunits, subunit structures, overview | Homo sapiens |
More | several isoforms for each of the three AMPK subunits, including alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, AMPKalpha subunit possesses a highly conserved, N-terminal catalytic domain that contains the activating phosphorylation site Thr172, an autoinhibitory domain, and a C-terminus that contains the domains required for binding with the beta and gamma subunits, subunit structures, overview | Rattus norvegicus |
trimer | in human skeletal muscle, the alpha2beta2gamma3 complexes constitute the majority of AMPK heterotrimers | Homo sapiens |
trimer | in rat skeletal muscle, the alpha2beta2gamma1 complexes constitute the majority of AMPK heterotrimers | Rattus norvegicus |
Synonyms | Comment | Organism |
---|---|---|
AMP-activated protein kinase | - |
Homo sapiens |
AMP-activated protein kinase | - |
Rattus norvegicus |
AMP-activated protein kinase | - |
Saccharomyces cerevisiae |
AMPK | - |
Homo sapiens |
AMPK | - |
Rattus norvegicus |
AMPK | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Homo sapiens | |
ATP | - |
Rattus norvegicus | |
ATP | - |
Saccharomyces cerevisiae |