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Enzyme Nomenclature
Information on EC 2.7.11.31 - [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase
for references in articles please use BRENDA:EC2.7.11.31
Word Map on EC 2.7.11.31
- 2.7.11.31
- diabetes
- rapamycin
- metformin
- aicar
- carboxylase
- peroxisome
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proliferator-activated
- obesity
- injury
- dysfunction
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autophagy
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adiponectin
- acetyl-coa
- cardiac
- glycogen
- adipocytes
- triglyceride
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high-fat
- hypothalamic
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antidiabetic
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3-kinase
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heterotrimeric
- 5-aminoimidazole-4-carboxamide
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ampk-dependent
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insulin-stimulated
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sirtuins
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p-ampk
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ampk-mediated
- ribonucleoside
- ampkalpha
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anti-obesity
- camkk
- 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside
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adipor1
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mtorc1
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transporter-4
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insulin-independent
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ampk-activating
- biguanide
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energy-sensing
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orexigenic
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phospho-ampk
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glucose-repressed
- drug development
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coactivator-1
- epitrochlearis
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substrate-1
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aicar-induced
- pharmacology
- industry
- medicine
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.11.31
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RECOMMENDED NAME
GeneOntology No.
[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphotransferase
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) [5]. Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase [7]. GTP can act instead of ATP [4]
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CAS REGISTRY NUMBER
COMMENTARY
172522-01-9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two alpha, two beta, and five gamma gene orthologues encoding the subunit variants
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644981, 644984, 662296, 665496, 690657, 690725, 691704, 692001, 692091, 692365, 692554, 693032, 693151, 693205, 693207, 693328, 694825, 701571, 701572, 701573, 702079, 703102, 703277, 703348, 703612, 704431, 704459, 704545, 705267, 705694, 705799, 705939, 706364, 706902
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644989, 665636, 687732, 690346, 691621, 692365, 693047, 694183, 701571, 701572, 701573, 701620, 702510, 703277, 703348, 703612, 703617, 704122, 704433, 704450, 705267, 705939, 706085
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286565, 491403, 644952, 644953, 644954, 644956, 644957, 644959, 644961, 644963, 644964, 644971, 644972, 644973, 644976, 644977, 644978, 644979, 644983, 644988, 663952, 665636, 684366, 690726, 691556, 691704, 692365, 692682, 693207, 701572, 701573, 703277, 703348, 704433, 705267, 705884, 705939
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male sprague-dawley rats
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beta subunit Gal83, equivalent to subunit beta 3
UniProt
beta subunit Sip1, equivalent to subunit beta 1
UniProt
beta subunit Sip2, equivalent to subunit beta 2
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the AMPK beta-subunit CBM has a beta-sandwich fold with the conserved residues Trp100, Lys126 and Trp133 (residue numbers according to beta1-CBM), classifying it under the CBM48 family; the AMPK beta-subunit CBM has a beta-sandwich fold with the conserved residues Trp100, Lys126 and Trp133 (residue numbers according to beta1-CBM), classifying it under the CBM48 family
evolution
the genes encoding the three subunits of AMPK are highly conserved in eukaryotic species for which complete genome sequences are available, including vertebrates, invertebrates, plants, fungi, and protozoa; the genes encoding the three subunits of AMPK are highly conserved in eukaryotic species for which complete genome sequences are available, including vertebrates, invertebrates, plants, fungi, and protozoa; the genes encoding the three subunits of AMPK are highly conserved in eukaryotic species for which complete genome sequences are available, including vertebrates, invertebrates, plants, fungi, and protozoa
evolution
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions; Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
evolution
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Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions; Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
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malfunction
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mice lacking either the alpha1 or alpha2 AMPK catalytic subunits demonstrate that AMPK is required for the effect of AICAR on glucose uptake. Transgenic mice expressing an inactive form of AMPK alpha2 subunit specifically in skeletal muscle develop impaired whole-body glucose tolerance and iInsulin resistance in skeletal muscle, particularly when fed a high-fat diet
malfunction
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mutations in the gamma2 and gamma3 subunits result in glycogen storage disease. Ten point mutations in gamma2 are associated with a glycogen storage cardiomyopathy and ventricular pre-excitation
malfunction
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in the liver from beta1 knockout mice the gamma1 subunit is present but alpha1 and alpha2 are degraded
malfunction
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mutations in the gamma2 and gamma3 subunits result in glycogen storage disease
malfunction
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AMPK gamma2 mutations are associated with hypertrophic cardiomyopathy
malfunction
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germline deletion of either AMPK beta1 or beta2 subunit isoforms results in reduced trabecular bone density and mass, but without effects on osteoclast or osteoblast numbers, as compared to wild-type littermate controls
malfunction
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Agouti-related peptide alpha2 AMPK-KO mice show decreased body weight even though there are no changes in food intake or energy expenditure and, the difference in body weight is lost when the animals are fed a high fat diet. Pro-opiomelanocortin alpha2 AMPK-KO animals show increased body weight and adiposity, which is further enhanced by a high fat diet
malfunction
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mice deficient in AMPKalpha-2 have smaller infarct volumes after middle cerebral artery occlusion, whereas AMPKalpha-1 deficiency has no effect compared to wild-type
malfunction
knockout of AMPKalpha1 enhances, and, conversely, activator A-769662 inhibits monosodium urate crystal-induced inflammatory responses including IL-1beta and CXCL1 release in vitro and in vivo
malfunction
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the absence of functional AMPK may consequently cause a failure of distinct signaling pathways in red bood cells
malfunction
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stabilization of MAPO1 occurs in AMPKalpha-knockdown cells even without N-methyl-N-nitrosourea treatment. Knockdown of the Flcn and Ampkalpha genes by specific siRNAs significantly suppresses an apoptotic response to N-methyl-N-nitrosourea
malfunction
deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2
malfunction
Mus musculus C57BL/6 / 129
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knockout of AMPKalpha1 enhances, and, conversely, activator A-769662 inhibits monosodium urate crystal-induced inflammatory responses including IL-1beta and CXCL1 release in vitro and in vivo
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malfunction
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germline deletion of either AMPK beta1 or beta2 subunit isoforms results in reduced trabecular bone density and mass, but without effects on osteoclast or osteoblast numbers, as compared to wild-type littermate controls
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malfunction
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deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2
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metabolism
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plays an important role in the regulation of both lipid and glucose metabolism. Direct link between AMPK activation and fatty acid metabolism. Has the potential of ameliorating insulin resistance and improving glucose homeostasis. A gain-of-function mutation in the gene encoding AMPK gamma3-subunit is reported to confer beneficial effects on muscle fuel metabolism
metabolism
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is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
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is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
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is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
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SNF1 protein kinase cascade, sharing functional similarities with mammalian AMPK, which plays an important role in adapting the unicellular eukaryote to glucose starvation
metabolism
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is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
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active AMPK promotes the functional recovery of beta-cell oxidative metabolism and abrogates the induction of pathways that mediate cell death such as caspase-3 activation following exposure to nitric oxide
metabolism
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is a metabolic energy regulator that can switch acid secretion off as cellular ATP levels fall. Secretagogue-induced acid secretion can be significantly reduced with AMPK activation and restored with its deactivation
physiological function
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role of AMPK is that it monitors cellular energy status by sensing the relative cellular concentrations of AMP and ATP. The beta-subunits of AMPK contain a glycogen-binding domain, which is a regulatory domain that allows AMPK to act as a sensor of the status of cellular reserves of energy in the form of glycogen. The pool of AMPK that is bound to the glycogen particle is in an active state when glycogen particles are fully synthesized, causing phosphorylation of glycogen synthase at site 2 and providing a feedback inhibition of further extension of the outer chains of glycogen
physiological function
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AMPK is responsible for phosphorylation of site 2 in vivo. Both basal and 5-aminoimidazole-4-carboxamide riboside (AICAR)-stimulated site 2 phosphorylation is greatly reduced in muscles of AMPK-alpha2 knockout mice
physiological function
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AMPK activation dramatically decreases de novo fatty acid synthesis and inactivates ACCalpha. AMPK activation modifies lipogenic gene expression including fatty acid synthase, glycerol-3-phosphate acyltransferase, and fatty acid binding protein-3. AMPK is able to inhibit fatty acid synthesis, an energy consuming process, in response to decreases in energy supply
physiological function
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activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease. Overexpression of AMPK increases cell viability after exposure to 1-methyl-4-pyridinium in SH-SY5Y cells
physiological function
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activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease
physiological function
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AMPK is required for proper cell division and faithful chromosomal segregation during mitosis. Active form of the alpha-catalytic AMPK subunit (P-AMPKalpha-Thr172), but not its total form (AMPKalpha), transiently associates with several mitotic structures including centrosomes, spindle poles, the central spindle midzone and the midbody throughout all of the mitotic stages and cytokinesis in human cancer-derived epithelial cells
physiological function
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AMPK may play an important role in protecting endothelial cells against adverse effects of sustained hyperglycaemia, such as alterations in fatty acid metabolism, impaired Akt activation by insulin, increased caspase 3 activity and apoptosis. It may modulate endothelial cell energy supply. The AMPK-acetyl CoA carboxylase-malonyl CoA-carnitine palmitoyl-transferase 1 mechanism for regulating long-chain fatty acid oxidation, similar to that of muscle, operates in the endothelial cell and is regulated by AMPK under physiological conditions. One way to deal with endothelial lipotoxicity is to promote free fatty acid oxidation and ameliorate lipid accumulation in endothelial cells, which can be achieved by activating endothelial AMPK. AMPK inhibits fatty acid-induced increases in NF-kappaB transactivation in cultured human umbilical vein endothelial cells
physiological function
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AMPK activation alters the expression of a variety of genes, including phosphoenolpyruvate carboxykinase in hepatocytes. Reduced AMPK activation may play an important role in the lipid accumulation and genesis of endothelial dysfunction in obese rats. Endothelial AMPK activity may inhibit glycerol-3-phosphate acyltransferase, required for de novo synthesis of diacylglycerol
physiological function
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AMPK activation inhibits TNFa-stimulated leukocyte adhesion to aortic endothelial cells and ICAM-1 mediated migration of lymphocytes across primary microvascular endothelial cells
physiological function
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AMPK activation induces vasodilatation and blood flow regulation in wild-type mice and this effect is abolished in AMPKalpha1 knockout mice. Chronic activation of AMPK in vivo attenuates ROS-mediated c-Jun N-terminal kinase activation and endothelial dysfunction in response to angiotensin II, which is abrogated in mice lacking the endothelial isoform of AMPKalpha1 or peroxisome proliferator gamma coactivator-1alpha, a target of AMPK that controls mitochondrial biogenesis. AMPK-deficient mice demonstrate impairment in postischemic fatty acid oxidation. In the setting of systolic pressure overload, left ventricular hypertrophy ensues and AMPKalpha2 knockout mice exhibit significantly increased overload-induced ventricular hypertrophy and decreased left ventricular ejection fraction. Isolated hearts of AMPK-deleted mice show increased apoptosis and dysfunction after ischemia/reperfusion. Role of AMPK in regulation of apoptosis that is an important mechanism of heart failure
physiological function
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AMPK activation inhibits ICAM-1 mediated migration of lymphocytes across primary microvascular endothelial cells
physiological function
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plays a crucial role in carbon catabolite repression in yeast. cRKIN1 gene product from rye can rescue SNF1 mutation
physiological function
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transgenic littermates overexpressing an alpha2AMPK kinase-dead (KD) have reduced skeletal muscle alpha2AMPK activity (50% in gastrocnemius and more than 80% in soleus and extensor digitorum longus) and acetyl-CoA carboxylase-2 Ser228 phosphorylation (90% in gastrocnemius). Obesity in response to high-fat feeding is not associated with impaired AMPK actions, obesity-induced lipid accumulation and insulin resistance are not exacerbated in AMPK KD mice
physiological function
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critical role of AMPK in the survival of circulating erythrocytes. As compared with erythrocytes from wild-type littermates (ampk+/+), erythrocytes from AMPKalpha1-deficient mice (ampk-/-) are significantly more susceptible to the eryptotic effect of energy depletion. The ampk-/- mice are anemic despite excessive reticulocytosis, and they suffer from severe splenomegaly
physiological function
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AMPK activation and subsequent increases in fatty acid beta-oxidation in skeletal muscle leads to increased energy expenditure in Uchl3-/- mice
physiological function
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AMPK is required to maintain normal bone density, but not through bone cell differentiation, and does not mediate powerful osteolytic effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
physiological function
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AMPK activation inhibits endothelial apoptosis in cultured cells. AMPK activation suppresses the basal and angiotensin II-enhanced superoxide anions in BAEC
physiological function
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overexpression or ablation of the AMPK gamma3 subunit does not appear to play a critical role in defining mitochondrial content in resting skeletal muscle. Skeletal muscle mitochondrial content is unaltered in AMPK gamma3-/- mice
physiological function
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AMPK activation during oxidative stress may switch retinal pigment epithelium cells to a self-protected status. Alpha2 but not alpha1 AMPK is involved in retinal pigment epithelium cell phagocytosis and activation of alpha2 AMPK contributes to the inhibition of retinal pigment epithelium cell phagocytosis by oxidative stress
physiological function
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role for AMPK, in concert with other signals induced by IFNgamma, in mediating reduced epithelial barrier function in a cell model of chronic intestinal inflammation
physiological function
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AMPK mediates cold-induced resistance to anorexigenic signalling in the hypothalamus. Activation of AMPK can contribute to hyperphagia. Inhibition of AMPK inhibits the hypoglycaemia-induced increase in the counter-regulatory hormones glucagon, corticosterone and catecholamines, causing a severe and prolonged hypoglycaemia
physiological function
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activation of AMPK alpha is necessary for hypoxia-induced AMPK-PKCzeta binding in alveolar epithelial cells. Overexpression of a dominant-negative AMPK alpha subunit construct prevents hypoxia-induced endocytosis of Na,K-ATPase, hypoxia-induced PKCzeta translocation to the plasma membrane and phosphorylation at Thr410
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor to maintain energy balance at both the cellular and the whole-body levels. The enzyme is activated under circumstances with an increased cellular AMP:ATP ratio, such as metabolic stresses that inhibit ATP production (hypoxia, glucose deprivation, metabolic inhibitors etc.) and those that stimulate ATP consumption (exercise, cell growth and division etc.)
physiological function
AMP-activated protein kinase (AMPK) is metabolic biosensor with anti-inflammatory activities. Gout is commonly associated with excesses in soluble urate and in nutrition, both of which suppress tissue AMPK activity. Gout is driven by macrophage-mediated inflammation transduced partly by NLRP3 inflammasome activation and interleukin-1beta release. AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages. Activated AMPK is anti-inflammatory partly through inhibition of NF-kappaB
physiological function
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AMPK is a metabolic stress-sensing kinase with important functions for red blood cell survival. Identification of putative AMPK targets in hemoglobin-depleted lysates of erythrocytes, including metabolic enzymes, cytoskeletal proteins and enzymes involved in the oxidative stress response, cloning and recombinant expression. AMPK aids the function of red blood cells
physiological function
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AMPK is a cellular energy sensor that negatively regulates cell growth and proliferation. MAPO1, identified as a component involved in the induction of apoptosis, is stabilized by interaction with AMP-activated protein kinase (AMPK) and folliculin (FLCN). AMPK is activated during the process of O6-methylguanine-induced apoptosis and this activation is dependent on MAPO1 and folliculin. It is likely that the kinase activity of AMPK is involved in the degradation of MAPO1
physiological function
Q13131 AND P54646
AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that serves as a pleotropic regulator of whole body energy homoeostasis. The enzyme is allosterically regulated, kinetic analysis, overview. Binding of activator AMP to the gamma-subunit allows a small regulatory segment of the alpha-subunit (alpha2 residues 365-371) called the alpha-hook or alpha-RIM2 to directly interact with bound AMP and create an allosteric conformational change at the catalytic active site. As a consequence, the phosphorylated alpha-Thr172/174 can be protected from dephosphorylation by phosphatases and sustain its kinase activity for an extended period
physiological function
sex-specific regulation of AMP-activated protein kinase alpha in the Pacific oyster Crassostrea gigas. AMPKalpha activation might play a sex-dependent role in management of energy during gametogenesis in oyster; sex-specific regulation of AMP-activated protein kinase in the Pacific oyster Crassostrea gigas; sex-specific regulation of AMP-activated protein kinase in the Pacific oyster Crassostrea gigas
physiological function
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress; Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress; Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2
physiological function
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AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that is essential in regulating energy metabolism in all eukaryotic cells
physiological function
Q13131 AND Q9Y478 AND P54619
ischemia stimulates the AMP-activated protein kinase (AMPK), a serine/threonine kinase, sensing energy depletion and stimulating several cellular mechanisms to enhance energy production and to limit energy utilization. AMPK downregulates the epithelial Na+ channel ENaC mediated by the ubiquitin ligase Nedd4-2. AMPK regulates the heterotetrameric K+-channel KCNQ1/KCNE1. Wild-type and constitutively active AMPK significantly reduce KCNQ1/KCNE1-mediated currents and reduce KCNQ1 abundance in the cell membrane of transfected Xenopus laevis oocytes, overview. AMPK decreased the KCNQ1 protein abundance in the cell membrane via ubiquitin ligase Nedd4-2
physiological function
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AMP-activated protein kinase (AMPK) maintains the balance between ATP production and energy consumption in eukaryotic cells by responding to the rise of intracellular AMP
physiological function
P54646 AND O43741 AND Q9UGI9
AMP-activated protein kinase (AMPK) is an energy-sensing serine/threonine protein kinase that plays a central role in whole-body energy homeostasis. The muscle-specific AMPK heterotrimeric complex (alpha2beta2gamma3) is involved in glucose and fat metabolism in skeletal muscle
physiological function
Mus musculus C57BL/6 / 129
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AMP-activated protein kinase (AMPK) is metabolic biosensor with anti-inflammatory activities. Gout is commonly associated with excesses in soluble urate and in nutrition, both of which suppress tissue AMPK activity. Gout is driven by macrophage-mediated inflammation transduced partly by NLRP3 inflammasome activation and interleukin-1beta release. AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages. Activated AMPK is anti-inflammatory partly through inhibition of NF-kappaB
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physiological function
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AMPK is required to maintain normal bone density, but not through bone cell differentiation, and does not mediate powerful osteolytic effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
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physiological function
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Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress; Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress; Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2
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additional information
the AMPK alpha2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the DFG-out conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter; the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter; the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter
additional information
Q13131 AND P54646
alpha1-subunit containing AMPK isoforms possess higher basal activity and are less sensitive to desphosphorylation by phosphatases compared with alpha2-subunit containing heterotrimers. The alpha2-subunit-containing complexes are more readily activated by AMP than alpha1-complexes. Enzymatic activity, phosphatase sensitivity and kinetics of alpha1- and alpha2-containing AMPK isoforms, differential effect of activators, overview
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
-
residues Glu42, Arg81, Asp156, and Phe175 of the isolated kinase domain fragment have greater conformational flexibility in the closed state, with the hinge residue Gly116 exhibiting two conformational basins in the closed state, and Gly115 already in an active-closed state conformation even when the interlobe conformation is open
additional information
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Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-hydroxy-3-methyl-glutaryl-CoA reductase
ADP + [3-hydroxy-3-methyl-glutaryl-CoA reductase]phosphate
-
-
-
-
?
ATP + 3-mercaptopyruvate sulfurtransferase
ADP + phosphorylated 3-mercaptopyruvate sulfurtransferase
-
-
-
?
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
-
-
-
-
?
ATP + acylamino-acid-releasing enzyme
ADP + phosphorylated acylamino-acid-releasing enzyme
-
-
-
?
ATP + adenylate kinase isoenzyme 1
ADP + phosphorylated adenylate kinase isoenzyme 1
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + adipose hormone-sensitive lipase phosphate
-
-
-
-
?
ATP + alpha,beta-tubulin
ADP + [alpha,beta-tubulin] phosphate
-
relative kinase activity high MW-kinase 15%
-
-
?
ATP + band 3 anion transport protein
ADP + phosphorylated band 3 anion transport protein
-
-
-
?
ATP + bis(5'-nucleosyl)-tetraphosphatase
ADP + [bis(5'-nucleosyl)-tetraphosphatase]phosphate
-
-
-
-
?
ATP + bisphosphoglycerate mutase
ADP + phosphorylated bisphosphoglycerate mutase
-
-
-
?
ATP + bovine serum albumin
ADP + [bovine serum albumin] phosphate
-
fraction V
-
-
?
ATP + carbonic anhydrase 1
ADP + phosphorylated carbonic anhydrase 1
-
-
-
?
ATP + collapsing response mediator protein-2
ADP + [collapsing response mediator protein-2]phosphate
-
-
-
-
?
ATP + Cy5-SAMS peptide
ADP + phosphorylated Cy5-SAMS peptide
P54646 AND O43741 AND Q9UGI9
-
-
-
?
ATP + cytoplasmic malate dehydrogenase
ADP + phosphorylated cytoplasmic malate dehydrogenase
-
-
-
?
ATP + dihydropteridine reductase
ADP + phosphorylated dihydropteridine reductase
-
-
-
?
ATP + dihydropyrimidinase-like 2
ADP + [dihydropyrimidinase-like 2]phosphate
-
-
-
-
?
ATP + DNA damage-binding protein 1
ADP + phosphorylated DNA damage-binding protein 1
-
-
-
?
ATP + dynein intermediate chain 2
ADP + [dynein intermediate chain 2]phosphate
-
-
-
-
?
ATP + erythrocyte spectrin alpha chain
ADP + phosphorylated erythrocyte spectrin alpha chain
-
-
-
?
ATP + erythrocyte spectrin beta chain
ADP + phosphorylated erythrocyte spectrin beta chain
-
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
ATP + far upstream element binding protein 1
ADP + [far upstream element binding protein 1]phosphate
-
-
-
-
?
ATP + glial fibrillary acidic protein
ADP + [glial fibrillary acidic protein]phosphate
-
-
-
-
?
ATP + glutamate dehydrogenase 1
ADP + [glutamate dehydrogenase 1]phosphate
-
-
-
-
?
ATP + glutathione S-transferase omega-1
ADP + phosphorylated glutathione S-transferase omega-1
-
-
-
?
ATP + glutathione synthetase
ADP + phosphorylated glutathione synthetase
-
-
-
?
ATP + glyceraldehyde-3-phosphate dehydrogenase
ADP + [glyceraldehyde-3-phosphate dehydrogenase]phosphate
-
-
-
-
?
ATP + glycerophosphate acyltransferase
ADP + [glycerophosphate acyltransferase]phosphate
-
-
-
-
?
ATP + glycogen synthase
ADP + [glycogen synthase] phosphate
-
relative kinase activity for low-MW kinase 7%, high MW-kinase 87%
-
-
?
ATP + heavy meromyosin
ADP + [heavy meromyosin] phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 100%
-
-
?
ATP + heterogeneous nuclear ribonucleoproteins A2/B1
ADP + [heterogeneous nuclear ribonucleoproteins A2/B1]phosphate
-
-
-
-
?
ATP + histone H1 (IIIS)
ADP + [histone H1 (IIIS)] phosphate
-
histones are better substrates for high-MW kinase than hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 275%, high MW-kinase 103%
-
-
?
ATP + histone II-S
ADP + [histone II-S] phosphate
-
relative kinase activity for low-MW kinase 38%, high MW-kinase 159%
-
-
?
ATP + histone VIIIS
ADP + [histone VIIIS] phosphate
-
relative kinase activity for low-MW kinase 65%, high MW-kinase 141%
-
-
?
ATP + HMKSAMSGLHLVKRR
ADP + ?
-
synthetic SAMS-containing peptide as substrate
-
-
?
ATP + MAP-2
ADP + MAP-2 phosphate
-
relative kinase activity for low-MW kinase 14%, high MW-kinase 566%
-
-
?
ATP + myelin basic protein
ADP + [myelin basic protein] phosphate
-
moderate substrate for low-MW kinase, better than hydroxymethylglutaryl-CoA reductase for high-MW kinase, relative kinase activity for low-MW kinase 36%, high MW-kinase 238%
-
-
?
ATP + myosin mixed light chains
ADP + [myosin mixed light chains] phosphate
-
relative kinase activity for low-MW kinase 4%, high MW-kinase 27%
-
-
?
ATP + neurofilament triplet L protein
ADP + [neurofilament triplet L protein]phosphate
-
-
-
-
?
ATP + Ngg1 interacting factor 3-like 1
ADP + [Ngg1 interacting factor 3-like 1]phosphate
-
-
-
-
?
ATP + NmrA-like family domain containing 1
ADP + [NmrA-like family domain containing 1]phosphate
-
-
-
-
?
ATP + PFK2
ADP + phospho-PFK2
-
phosphorylation at Ser466 induced by UV radiation and H2O2 treatment
-
-
?
ATP + phosphoglycerate kinase 1
ADP + phosphorylated phosphoglycerate kinase 1
-
-
-
?
ATP + phosphoribosylformylglycinamidine synthase
ADP + phosphorylated phosphoribosylformylglycinamidine synthase
-
-
-
?
ATP + phosphorylase B
ADP + [phosphorylase B] phosphate
-
relative kinase activity high MW-kinase 12%
-
-
?
ATP + PKZeta
?
-
AMPK alpha phosphorylates PKZeta on residue Thr410 within the PKCzeta activation loop
-
-
?
ATP + proteasome subunit alpha type-1
ADP + phosphorylated proteasome subunit alpha type-1
-
-
-
?
ATP + proteasome subunit alpha type-7
ADP + phosphorylated proteasome subunit alpha type-7
-
-
-
?
ATP + protein kinase C and casein kinase substrate in neurons protein 1
ADP + [protein kinase C and casein kinase substrate in neurons protein 1]phosphate
-
-
-
-
?
ATP + purine nucleoside phosphorylase
ADP + phosphorylated purine nucleoside phosphorylase
-
-
-
?
ATP + rabbit muscle glycogen synthase
ADP + [rabbit muscle glycogen synthase] phosphate
-
rabbit muscle glycogen synthase
-
-
?
ATP + RNA-binding protein HUR
ADP + ?
-
inhibits the protein by phosporylation
-
-
?
ATP + S-formylglutathione hydrolase
ADP + phosphorylated S-formylglutathione hydrolase
-
-
-
?
ATP + selenium binding protein 1
ADP + phosphorylated selenium binding protein 1
-
-
-
?
ATP + synapsin 1
ADP + [synapsin 1] phosphate
-
as good substrate as hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 151%, high MW-kinase 103%
-
-
?
ATP + telomerase-binding protein p23
ADP + [telomerase-binding protein p23]phosphate
-
-
-
-
?
ATP + thioredoxin-like protein 1
ADP + phosphorylated thioredoxin-like protein 1
-
-
-
?
ATP + tripeptidyl-peptidase 2
ADP + [tripeptidyl-peptidase 2]phosphate
-
-
-
-
?
ATP + ubiquitin carboxyl-terminal hydrolase 13
ADP + phosphorylated ubiquitin carboxyl-terminal hydrolase 13
-
-
-
?
ATP + ubiquitin carboxyl-terminal hydrolase 14
ADP + phosphorylated ubiquitin carboxyl-terminal hydrolase 14
-
-
-
?
ATP + ubiquitin carboxyl-terminal hydrolase 5
ADP + phosphorylated ubiquitin carboxyl-terminal hydrolase 5
-
-
-
?
ATP + ubiquitin-activating enzyme E1
ADP + phosphorylated ubiquitin-activating enzyme E1
-
-
-
?
ATP + valosin-containing protein
ADP + phosphorylated valosin-containing protein
-
-
-
?
ATP + [acetyl-CoA carboxylase 2]
ADP + [acetyl-CoA carboxylase 2] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + phospho-[acetyl-CoA carboxylase]
-
phosphorylation at Ser79
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
ATP + [eukaryotic elongation factor-2]
ADP + [eukaryotic elongation factor-2] phosphate
-
phosphorylation at Ser259 and Ser498
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + [peptide QKFQRELSTKWVLN]
ADP + [peptide QKFQRELSTKWVLN] phosphate
-
a peptide derived from glucose hexokinase regulatory protein, residues 474-487
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
CTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
CDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
dATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
dADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 90% the rate of ATP
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
the enzyme is involved in the regulation of hepatic lipids via its downstream effector acetyl-CoA carboxylase, enzyme inhibition leads to an increased level of triacylglycerols and accumulation of lipids, metformin decreases lipid accumulation, induced by high D-glucose levels, by activating the enzyme, the enzyme functions as energy intracellular sensor
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
phosphorylation at Ser79, phosphorylation inhibits the acetyl-CoA carboxylase
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
phosphorylation at Ser79
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
AMPK plays an important role in regulating malonyl-CoA levels through the phosphorylation of acetyl-CoA carboxylase
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
substrate Rattus norvegicus hepatic acetyl-CoA carboxylase, enzyme phosphorylates Ser-residues 79, 1200 and 1215
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
AMPK alpha phosphorylates at Ser79
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
AMPKalpha can phosphorylate Ser79 of acetyl-CoA carboxylase
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + [adipose hormone-sensitive lipase] phosphate
-
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + [adipose hormone-sensitive lipase] phosphate
-
-
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
phosphorylation at Ser63 and Ser267, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + ATF2
ADP + phospho-ATF2
-
recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + biotin-GGHMRSAMSGLHLVKRR-NH2
ADP + phosphorylated biotin-GGHMRSAMpSGLHLVKRR-NH2
-
i.e. SAMS peptide, a peptide derived from residues 73-85 of rat acetyl-CoA carboxylase in which Ser77 is mutated to Ala and the AMPK phosphorylation site is Ser79
-
-
?
ATP + biotin-GGHMRSAMSGLHLVKRR-NH2
ADP + phosphorylated biotin-GGHMRSAMpSGLHLVKRR-NH2
Q13131 AND P54646
i.e. SAMS peptide, a peptide derived from residues 73-85 of rat acetyl-CoA carboxylase in which Ser77 is mutated to Ala and the AMPK phosphorylation site is Ser79
-
-
?
ATP + casein
ADP + casein phosphate
-
relative kinase activity for low-MW kinase 8%, high MW-kinase 48%
-
-
?
ATP + casein
ADP + casein phosphate
-
relative kinase activity for low-MW kinase 8%, high MW-kinase 48%
-
-
?
ATP + CREB
ADP + phospho-CREB
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREB
ADP + phospho-CREB
-
phosphorylation at Ser98 and Ser133, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREB1
ADP + phospho-CREB1
-
AMPK competes with protein kinase A for the Ser119 phosphorylation site
-
-
?
ATP + CREB1
ADP + phospho-CREB1
-
phosphorylation at Ser119, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREBL2
ADP + phospho-CREBL2
-
recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREM
ADP + phospho-CREM
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREM
ADP + phospho-CREM
-
phosphorylation at Ser71 and Ser192, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
-
phosphorylation at Ser398, the enzyme plays a regulatory role in eEF2 kinase activity, overview
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
-
phosphorylation at Ser398 activates the eukaryotic elongation factor 2 kinase, no activity with the substrate mutant S398A
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
synthetic SAMS-containing peptide as substrate
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
acetyl-CoA carboxylase-derived synthetic peptide substrate
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
acetyl-CoA carboxylase-derived synthetic peptide substrate
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcription factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcriptions factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcriptions factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcription factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
a zinc-finger transcriptions factor, the Gal83 isoform is necessary and sufficient for phosphorylation of Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
a zinc-finger transcriptions factor, the Gal83 isoform is necessary and sufficient for phosphorylation of Mig2
-
-
?
ATP + p27
ADP + phospho-p27
-
loss of tuberin is associated with increased AMPK activity and altered p27 function leading to increased Cdk2 activity and resistance of the cells against apoptosis. Mislocation of p27 occurs in tuberin-deficient cells, possessing no functional gene tsc2, and can induced directly by activating AMPK physiologically via glucose deprivation or genetically via a constitutively active AMPK, overview
-
-
?
ATP + p27
ADP + phospho-p27
-
AMPK phosphorylates p27 function at least at three sites, Thr172, Thr170, and Ser83, Thr170 is localized near the nuclear localization signal sequence and its phosphorylation is responsible for p27 translocation to the cytoplasm
-
-
?
ATP + p38
ADP + phospho-p38
-
phosphorylation at Thr180/Thr182, p38 MAPK is a downstream signal of AMPK upon various stimuli, AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + p53
ADP + phospho-p53
-
AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 2%
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 2%
-
-
?
ATP + protamine
ADP + protamine phosphate
-
relative kinase activity for low-MW kinase 24%, high MW-kinase 38%
-
-
?
ATP + protamine
ADP + protamine phosphate
-
relative kinase activity for low-MW kinase 24%, high MW-kinase 38%
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131 AND Q9Y478 AND P54619
-
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131 AND Q9Y478 AND P54619
activation
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inhibition of acetyl-CoA carboxylase
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
-
activates nitric oxide synthesis, mechanism, overview
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
-
phosphorylation by AMPK at Ser1177
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
AMPK-eNOS signalling, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
phosphorylation at Ser1177
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
-
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
-
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
phosphorylation by AMPK at a site in residues 474-487
-
-
?
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
-
phosphorylation at Thr1337 to induce disassembly of Golgi apparatus
-
-
?
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
-
a guanine nucleotide exchange factor for the ADP-ribosylation factor family associated with the Golgi apparatus, phosphorylation at Thr1337, phosphorylation site identification by mutational analysis
-
-
?
ATP + [histone deacetylase 5]
ADP + [histone deacetylase 5] phosphate
-
AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
-
-
?
ATP + [histone deacetylase 5]
ADP + [histone deacetylase 5] phosphate
-
phosphorylation at Ser259 and Ser498
-
-
?
ATP + [HMG-CoA reductase]
ADP + [HMG-CoA reductase] phosphate
-
-
-
-
?
ATP + [HMG-CoA reductase]
ADP + [HMG-CoA reductase] phosphate
-
inhibition of HMG-CoA carboxylase
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
2 isoforms, major form A and minor form B, both phosphorylates mammalian HMG-CoA reductase
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
-
-
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
activated AMPK acts to down-regulate ATP-consuming pathways such as fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase and protein synthesis by promoting the phosphorylation of eukaryotic elongation factor-2, in heart AMPK activation stimulates glycolysis by increasing glucose uptake
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
bicyclic phosporylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [malonylCoAdecarboxylase]
ADP + [malonylCoAdecarboxylase]phosphate
-
-
-
-
?
ATP + [malonylCoAdecarboxylase]
ADP + [malonylCoAdecarboxylase]phosphate
-
-
-
-
?
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
-
activation
-
-
?
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
-
AMP-activated protein kinase activates O-glucosaminyl-acylation of neuronal proteins, e.g. neurofilament H, during glucose deprivation involving activation of O-GlcNAc transferase, OGT, and induces OGT protein expression in Neuro-2a neuroblastoma cells, mechanism, overview
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
-
i.e. SAMS peptide
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
-
i.e. SAMS peptide
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
i.e. SAMS peptide
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
-
phosphorylation activates MLCK and increases its affinity for Ca2+ and calmodulin
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
-
phosphorylation in the CaM-binding domain at Ser815, substrate from chicken, determination of the phosphorylation site by mass spectrometric analysis
-
-
?
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
-
-
-
-
?
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
-
-
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 30% the rate of ATP
-
-
?
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 10% the rate of ATP
-
-
?
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 5% the rate of ATP
-
-
?
additional information
?
-
-
AMPK can influence the behavior of Caenorhabditis elegans worms in addition to its well known function in metabolic control, aak-1 and aak-2 affect paraquat sensitivity of adult worms, overview
-
-
-
additional information
?
-
-
AMPK promotes ATP production and inhibits ATp consumption acting as a metabolic switch, mechanism, overview. AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals, AMPK signaling pathways, overview
-
-
-
additional information
?
-
-
enzyme functions as a metabolic sensor that monitors cellular AMP and ATP levels
-
-
-
additional information
?
-
-
conditions that elevate the AMP:ATP ratio in cells, such as growth factor depletion, hypoglycemia, ischemia in heart muscle, exercise in skeletal muscle, as well as treatment with arsenite, azide, oxidative agents and the pharmacological agent AICAR, which mimics the effect of AMP can cause activation of AMPK
-
-
-
additional information
?
-
-
phosphorylates key target proteins that control flux through metabolic pathways of hepatic ketogenesis, cholesterol synthesis, adipocyte lipolysis and skeletal muscle fatty acid oxidation
-
-
-
additional information
?
-
-
AMP-activated protein kinase acts as a key energy sensor in regulating intracellular lysosomal protein degradation and is involved in proteasomal degradation of proteins, which allows the regulation of proteasomal activity under conditions of energy demand, mechanism, overview
-
-
-
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
-
-
-
additional information
?
-
-
AMP-activated protein kinase contributes to UV- and H2O2-induced apoptosis in human skin keratinocytes, AMPK serves as a negative feedback signal against UV-induced mammalian target of rapamycin, mTOR activation in a TSC2-dependent manner, AMPK plays important roles in UV-induced signal transduction ultimately leading to skin photoaging and even skin cancer, regulation, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase is involved in 8-chloro-cAMP-induced growth inhibition which proceeds via p38 MAPK and the metabolite 8-chloro-adenosine, AICAR must be phosphorylated to ZMP by adenosine kinases in order to activate AMPK, mechanism, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase is involved in regulation of the activation of the PGC-1alpha promoter and PGC-1alpha expression in skeletal muscle cells, effect of AMPK activation on DNA binding and protein expression, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes representing a mechanism in Cushings syndrome, overview. activation of AMPK stimulates appetite in the hypothalamus and stimulates catabolic processes in the periphery
-
-
-
additional information
?
-
-
AMPK is a sensor of the cellular energy status, it also exerts modulation of the fibrogenic properties of hepatic stellate cells, physiological effects of AMPK activation and inhibition, mechanism, AMPK activation regulates intracellular signaling pathways in hepatic stellate cells, overview
-
-
-
additional information
?
-
-
AMPK is activated in response to changes in the cellular energy charge and cellular stress via increases in the ATP-to-AMP ratio
-
-
-
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
-
additional information
?
-
-
AMPK signaling influences glucose and lipid metabolisms, mitochondrial biogenesis, and gene transcription, playing a role in trained and obese physiological state, overview. AMPK is important in the molecular regulation of lipid oxidation in skeletal muscle and the energy balance through suppression of ATP-consuming anabolic pathways and enhancement of ATP-producing catabolic pathways, overview
-
-
-
additional information
?
-
-
lovostatin-induced endothelial progenitor cell to endothelial cell differentiation depends on AMPK, AMPK enhances the vasculogensis and angiogenesis of endothelial progenitor cells, overview
-
-
-
additional information
?
-
-
AMPK phosphorylates histone deacetylase 5 (HDAC5) at Ser259 and Ser498 in primary myocytes
-
-
-
additional information
?
-
-
AMPK phosphorylates site 2 on glycogen synthase in cell-free assays
-
-
-
additional information
?
-
identification of putative AMPK targets in hemoglobin-depleted lysates of erythrocytes, including metabolic enzymes, cytoskeletal proteins and enzymes involved in the oxidative stress response, cloning and recombinant expression
-
-
-
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase acts as an energy sensor able to adapt cellular metabolism in response to nutritional environmental variations, and it regulates lymphocyte responses to metabolic stress but is largely dispensable for immune cell development and function, overview
-
-
-
additional information
?
-
-
AMPK and calcineurin, a calcium-regulated serine/threonine protein phosphatase, regulate skeletal muscle metabolic gene expression programs in response to changes in the energy status and levels of neuronic input, respectively. AMPK activates metabolic genes, mitochondrial biogenesis, glucose uptake, lipid oxidation, and insulin sesitivity, but blocks protein synthesis, pathway and regulation, overview
-
-
-
additional information
?
-
-
AMPK is a regulator of gene transcription increasing mitochondrial proteins of oxidative metabolsim as well as hexokinase expression in muscles
-
-
-
additional information
?
-
-
AMPK is an important energy-sensing protein in skeletal muscle, it inhibits mTOR signaling thereby inhibiting protein synthesis initiation via S6K1 and 4E-BP1, regulation system, overview
-
-
-
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
-
additional information
?
-
-
AMP-activated protein kinase phosphorylates transcription factors of the CREB family
-
-
-
additional information
?
-
-
AMPK signalling pathways are downregulated and skeletal muscle development is impaired in fetuses of obese, over-nourished sheep without differences in energy status, i.e. the AMP/ATP ratio, overview. Decreased signalling of the AMPK system in skeletal muscle of fetuses of OB mothers may play a role in altered muscle development and development of insulin resistance in the offspring
-
-
-
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
-
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
-
additional information
?
-
-
protein kinase C and Ca2+/calmodulin dependent reductase kinases are no substrates
-
-
-
additional information
?
-
-
incorporates 0.5 mol phosphate/mol MW 53000 enzyme substrate fragment, 2 mol phosphate/mol native enzyme substrate
-
-
-
additional information
?
-
-
acetyl-CoA carboxylase kinase EC 2.7.1.128 and hydroxymethylglutaryl-CoA reductase kinase activity are catalyzed by the same enzyme
-
-
-
additional information
?
-
-
regulates triacylglycerolsynthesis and fatty acid oxidation in liver and muscle reciprocally
-
-
-
additional information
?
-
-
AMPK regulation, AMPK mediates the autophagy suppression of okadaic acid and other protein phosphatase-inhibitory toxins, overview
-
-
-
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
-
additional information
?
-
-
the enzyme is regulated by the nucleoside diphosphate kinase, complex formation in vivo, e.g. between isozyme alpha1 and NDPK-H1, inhibits the enzyme, overview
-
-
-
additional information
?
-
-
activation of AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis. AMPK mediates CO2-induced Na,K-ATPase endocytosis and alveolar epithelial dysfunction, which can be prevented with beta-adrenergic agonists and cAMP
-
-
-
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
-
-
-
additional information
?
-
-
AMP-activated protein kinase is essential for survival in chronic hypoxia
-
-
-
additional information
?
-
-
AMPK inhibits hepatioc lipogenesis through multisite control, involving inhibition of glucose hexokinase translocation with consequent inhibition of flux through glucose phosphorylation and glycolysis, overview
-
-
-
additional information
?
-
-
AMPK is a cellular energy sensor that is activated during mitochondrial inhibition and shuts down biosynthetic processes to help conserve cellular ATP levels
-
-
-
additional information
?
-
-
AMPK plays a central role in the regulation of lipid metabolism, AMPK activity may have an important role in the development of alcoholic fatty liver, AMPK activator AICAR strongly inhibits the activity of acetyl-CoA carboxylase in hepatocyte preparations in parallel to fatty acid synthesis, but cells from ethanol-fed rats show significantly lower sensitivity to inhibition by AICAR, overview
-
-
-
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
-
additional information
?
-
-
anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
-
-
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
-
hypoxic pulmonary vasoconstriction is precipitated, at least in part, by the inhibition of mitochondrial oxidative phosphorylation by hypoxia, an increase in the AMP/ATP ratio and consequent activation of AMP-activated protein kinase, mechanism, overview
-
-
-
additional information
?
-
-
key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
-
-
-
additional information
?
-
-
neuronal AMPK responds to cellular energy requirements as well as whole body energy demands, mechanism, in patholgical brain AMPK responds globally in the brain to energy challenge, while in healthy brain only to changes in energy balance/food/intake, increased AMPK activity leads to inhibition of energy-using processes and, during ischemia, can lead to complete energy failure and death by stroke, overview. AMPK mediates the physiological effects of C75, an alpha-methylene-gamma-butyrolactone beta-ketoacyl synthase inhibitor, brain injection of C75 increases ATP levels in neurons, glucose oxidation FAS activity, CPT-1 activity, food intake and body weight in rodents, detailed overview
-
-
-
additional information
?
-
-
the thrifty metabolism that favors fat storage after caloric restriction involves AMPK activity, AMPK signaling is diminished during refeeding after caloric restriction rats. Isocaloric refeeding with a high-fat diet, which exacerbates the suppression of thermogenesis, results in further reduction and in impaired AMPK phosphorylation, overview
-
-
-
additional information
?
-
-
AMPK promotes reactivation of mitochondrial aconitase
-
-
-
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
-
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
-
additional information
?
-
-
incorporates 0.5 mol phosphate/mol MW 53000 enzyme substrate fragment, 2 mol phosphate/mol native enzyme substrate
-
-
-
additional information
?
-
-
regulates triacylglycerolsynthesis and fatty acid oxidation in liver and muscle reciprocally
-
-
-
additional information
?
-
-
acetyl-CoA carboxylase kinase EC 2.7.1.128 and hydroxymethylglutaryl-CoA reductase kinase activity are catalyzed by the same enzyme
-
-
-
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
-
-
-
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
-
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
-
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
-
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
-
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
-
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
-
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
-
Snf4 subunit contains cystathionine-beta-synthase (CBS) sequence repeats. CBS4 can be occupied either by AMP, ZMP or ATP, and CBS2 by ADP
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
-
-
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREB
ADP + phospho-CREB
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREB1
ADP + phospho-CREB1
-
AMPK competes with protein kinase A for the Ser119 phosphorylation site
-
-
?
ATP + CREM
ADP + phospho-CREM
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
-
phosphorylation at Ser398, the enzyme plays a regulatory role in eEF2 kinase activity, overview
-
-
?
ATP + p27
ADP + phospho-p27
-
loss of tuberin is associated with increased AMPK activity and altered p27 function leading to increased Cdk2 activity and resistance of the cells against apoptosis. Mislocation of p27 occurs in tuberin-deficient cells, possessing no functional gene tsc2, and can induced directly by activating AMPK physiologically via glucose deprivation or genetically via a constitutively active AMPK, overview
-
-
?
ATP + p38
ADP + phospho-p38
-
phosphorylation at Thr180/Thr182, p38 MAPK is a downstream signal of AMPK upon various stimuli, AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + p53
ADP + phospho-p53
-
AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + PFK2
ADP + phospho-PFK2
-
phosphorylation at Ser466 induced by UV radiation and H2O2 treatment
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131 AND Q9Y478 AND P54619
activation
-
-
?
ATP + [acetyl-CoA carboxylase 2]
ADP + [acetyl-CoA carboxylase 2] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + phospho-[acetyl-CoA carboxylase]
-
phosphorylation at Ser79
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
-
activates nitric oxide synthesis, mechanism, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
-
-
-
?
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
-
phosphorylation at Thr1337 to induce disassembly of Golgi apparatus
-
-
?
ATP + [histone deacetylase 5]
ADP + [histone deacetylase 5] phosphate
-
AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
-
-
?
ATP + [HMG-CoA reductase]
ADP + [HMG-CoA reductase] phosphate
-
inhibition of HMG-CoA carboxylase
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
-
AMP-activated protein kinase activates O-glucosaminyl-acylation of neuronal proteins, e.g. neurofilament H, during glucose deprivation involving activation of O-GlcNAc transferase, OGT, and induces OGT protein expression in Neuro-2a neuroblastoma cells, mechanism, overview
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
-
phosphorylation activates MLCK and increases its affinity for Ca2+ and calmodulin
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
the enzyme is involved in the regulation of hepatic lipids via its downstream effector acetyl-CoA carboxylase, enzyme inhibition leads to an increased level of triacylglycerols and accumulation of lipids, metformin decreases lipid accumulation, induced by high D-glucose levels, by activating the enzyme, the enzyme functions as energy intracellular sensor
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
P32578, P34164, Q04739
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
P32578, P34164, Q04739
-
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
P32578, P34164, Q04739
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
P32578, P34164, Q04739
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inhibition of acetyl-CoA carboxylase
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
AMPK-eNOS signalling, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
-
-
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
activated AMPK acts to down-regulate ATP-consuming pathways such as fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase and protein synthesis by promoting the phosphorylation of eukaryotic elongation factor-2, in heart AMPK activation stimulates glycolysis by increasing glucose uptake
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
bicyclic phosporylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
additional information
?
-
-
AMPK can influence the behavior of Caenorhabditis elegans worms in addition to its well known function in metabolic control, aak-1 and aak-2 affect paraquat sensitivity of adult worms, overview
-
-
-
additional information
?
-
-
AMPK promotes ATP production and inhibits ATp consumption acting as a metabolic switch, mechanism, overview. AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals, AMPK signaling pathways, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase acts as a key energy sensor in regulating intracellular lysosomal protein degradation and is involved in proteasomal degradation of proteins, which allows the regulation of proteasomal activity under conditions of energy demand, mechanism, overview
-
-
-
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
-
-
-
additional information
?
-
-
AMP-activated protein kinase contributes to UV- and H2O2-induced apoptosis in human skin keratinocytes, AMPK serves as a negative feedback signal against UV-induced mammalian target of rapamycin, mTOR activation in a TSC2-dependent manner, AMPK plays important roles in UV-induced signal transduction ultimately leading to skin photoaging and even skin cancer, regulation, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase is involved in 8-chloro-cAMP-induced growth inhibition which proceeds via p38 MAPK and the metabolite 8-chloro-adenosine, AICAR must be phosphorylated to ZMP by adenosine kinases in order to activate AMPK, mechanism, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase is involved in regulation of the activation of the PGC-1alpha promoter and PGC-1alpha expression in skeletal muscle cells, effect of AMPK activation on DNA binding and protein expression, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes representing a mechanism in Cushings syndrome, overview. activation of AMPK stimulates appetite in the hypothalamus and stimulates catabolic processes in the periphery
-
-
-
additional information
?
-
-
AMPK is a sensor of the cellular energy status, it also exerts modulation of the fibrogenic properties of hepatic stellate cells, physiological effects of AMPK activation and inhibition, mechanism, AMPK activation regulates intracellular signaling pathways in hepatic stellate cells, overview
-
-
-
additional information
?
-
-
AMPK is activated in response to changes in the cellular energy charge and cellular stress via increases in the ATP-to-AMP ratio
-
-
-
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
-
additional information
?
-
-
AMPK signaling influences glucose and lipid metabolisms, mitochondrial biogenesis, and gene transcription, playing a role in trained and obese physiological state, overview. AMPK is important in the molecular regulation of lipid oxidation in skeletal muscle and the energy balance through suppression of ATP-consuming anabolic pathways and enhancement of ATP-producing catabolic pathways, overview
-
-
-
additional information
?
-
-
lovostatin-induced endothelial progenitor cell to endothelial cell differentiation depends on AMPK, AMPK enhances the vasculogensis and angiogenesis of endothelial progenitor cells, overview
-
-
-
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
-
additional information
?
-
-
AMP-activated protein kinase acts as an energy sensor able to adapt cellular metabolism in response to nutritional environmental variations, and it regulates lymphocyte responses to metabolic stress but is largely dispensable for immune cell development and function, overview
-
-
-
additional information
?
-
-
AMPK and calcineurin, a calcium-regulated serine/threonine protein phosphatase, regulate skeletal muscle metabolic gene expression programs in response to changes in the energy status and levels of neuronic input, respectively. AMPK activates metabolic genes, mitochondrial biogenesis, glucose uptake, lipid oxidation, and insulin sesitivity, but blocks protein synthesis, pathway and regulation, overview
-
-
-
additional information
?
-
-
AMPK is a regulator of gene transcription increasing mitochondrial proteins of oxidative metabolsim as well as hexokinase expression in muscles
-
-
-
additional information
?
-
-
AMPK is an important energy-sensing protein in skeletal muscle, it inhibits mTOR signaling thereby inhibiting protein synthesis initiation via S6K1 and 4E-BP1, regulation system, overview
-
-
-
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
-
additional information
?
-
-
AMPK signalling pathways are downregulated and skeletal muscle development is impaired in fetuses of obese, over-nourished sheep without differences in energy status, i.e. the AMP/ATP ratio, overview. Decreased signalling of the AMPK system in skeletal muscle of fetuses of OB mothers may play a role in altered muscle development and development of insulin resistance in the offspring
-
-
-
additional information
?
-
-
AMPK regulation, AMPK mediates the autophagy suppression of okadaic acid and other protein phosphatase-inhibitory toxins, overview
-
-
-
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
-
additional information
?
-
-
activation of AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis. AMPK mediates CO2-induced Na,K-ATPase endocytosis and alveolar epithelial dysfunction, which can be prevented with beta-adrenergic agonists and cAMP
-
-
-
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
-
-
-
additional information
?
-
-
AMP-activated protein kinase is essential for survival in chronic hypoxia
-
-
-
additional information
?
-
-
AMPK inhibits hepatioc lipogenesis through multisite control, involving inhibition of glucose hexokinase translocation with consequent inhibition of flux through glucose phosphorylation and glycolysis, overview
-
-
-
additional information
?
-
-
AMPK is a cellular energy sensor that is activated during mitochondrial inhibition and shuts down biosynthetic processes to help conserve cellular ATP levels
-
-
-
additional information
?
-
-
AMPK plays a central role in the regulation of lipid metabolism, AMPK activity may have an important role in the development of alcoholic fatty liver, AMPK activator AICAR strongly inhibits the activity of acetyl-CoA carboxylase in hepatocyte preparations in parallel to fatty acid synthesis, but cells from ethanol-fed rats show significantly lower sensitivity to inhibition by AICAR, overview
-
-
-
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
-
additional information
?
-
-
anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
-
-
additional information
?
-
P54645
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
P80385
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
P80386
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
Q09137
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
-
additional information
?
-
-
hypoxic pulmonary vasoconstriction is precipitated, at least in part, by the inhibition of mitochondrial oxidative phosphorylation by hypoxia, an increase in the AMP/ATP ratio and consequent activation of AMP-activated protein kinase, mechanism, overview
-
-
-
additional information
?
-
-
key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
-
-
-
additional information
?
-
-
neuronal AMPK responds to cellular energy requirements as well as whole body energy demands, mechanism, in patholgical brain AMPK responds globally in the brain to energy challenge, while in healthy brain only to changes in energy balance/food/intake, increased AMPK activity leads to inhibition of energy-using processes and, during ischemia, can lead to complete energy failure and death by stroke, overview. AMPK mediates the physiological effects of C75, an alpha-methylene-gamma-butyrolactone beta-ketoacyl synthase inhibitor, brain injection of C75 increases ATP levels in neurons, glucose oxidation FAS activity, CPT-1 activity, food intake and body weight in rodents, detailed overview
-
-
-
additional information
?
-
-
the thrifty metabolism that favors fat storage after caloric restriction involves AMPK activity, AMPK signaling is diminished during refeeding after caloric restriction rats. Isocaloric refeeding with a high-fat diet, which exacerbates the suppression of thermogenesis, results in further reduction and in impaired AMPK phosphorylation, overview
-
-
-
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
-
-
-
additional information
?
-
P32578
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
P34164
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
Q04739
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
P32578
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
P34164
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
additional information
?
-
Q04739
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
-
requirement, Ca2+/calmodulin dependent kinase, no phosphorylation of substrate observed in absence
AMP
-
dependent on, AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
-
increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview
Ca2+
-
AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
Ca2+
-
increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview
Ca2+
-
activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
Mg2+
-
-
Mg2+
-
Asp-157 within the DFG motif is required for binding the Mg2+ ion that co-ordinates beta and gamma phosphates of Mg2+-ATP in the active site
Mg2+
-
requirement, actual substrate: MgATP2-
Mg2+
-
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
A134974
-
at 1 nM ablates the stimulatory action of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside with no effects on osteoclast formation in the absence of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
adenosine-5'-tetraphospho-5'-adenosine
-
i.e. AP4A, inhibits in the presence of AMP
C75
-
rapidly reduces the level of the phosphorylated AMPKalpha subunit in the hypothalamus. Also reduces pAMPK levels in fasted mice that have elevated hypothalamic pAMPK
Cu2+
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
dexamethasone
-
decreases in AMPK activity in treated adipocytes. The inhibitory effect of dexamethasone on AMPK activity is antagonized by co-administration of metformin at 0.01 mM, which increases AMPK activity to 224% compared with dexamethasone treatment alone
hydroxymethylglutaryl-CoA
-
only with hydroxymethylglutaryl-CoA reductase as substrate
leptin
-
has a tissue-specific effect on AMPK, in the hypothalamus, it decreases hypothalamic AMPK activity
-
metformin
-
can inhibit the stimulatory effect of dexamethasone in primary hypothalamic culture, blocks the AMPK phosphorylation induced by low glucose in primary cultures of hypothalamic neurones
nicotinamide
-
SIRT1 inhibitor, potentiates Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation. Potentiates Tat-induced HIV-1 transactivation
propranolol
-
effects of interleukin-6 on both AMPK activity and energy state are inhibited by coincubation with propranolol, suggesting involvement of beta-adrenergic signaling
STO 609
molecular docking study, STO 609 docks in the compound-C binding pocket of AMPK
Sucrose
-
sucrose-drinking animals have lower hypothalamic AMPK activity compared to saline-drinking control rats
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, abolishes statin-induced reduction of O2- in BAEC
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, potent AMPK inhibitor, inhibition results in an increase in 1-methyl-4-pyridinium-induced cell death. Prevents the AMPK activation by 1-methyl-4-pyridinium and stimulates 1-methyl-4-pyridinium-induced cell death
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, AMPK-inhibitor, 0.02 mM does not significantly modify eryptosis under glucose-replete conditions but significantly augments the eryptotic effect of glucose withdrawal
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, inhibition of AMPK prevents at 0.05 mM, in part, the IFNgamma-induced decrease in transepithelial electrical resistance, the increased epithelial permeability, the decreased transepithelial electrical resistance, and the decrease in occludin and zonula occludens-1 caused by IFNgamma treatment of T84 cells
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, hypoxia-induced PKCzeta translocation to the plasma membrane and phosphorylation at Thr410 is prevented by pharmacological inhibition of AMPK
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, AMPK inhibitor, reduces puerarin-induced suppression of MDR1 expression
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, potentiates Tat-induced HIV-1 transactivation
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, at a concentration of 0.02 mM, suppresses the glucose-stimulated rise in cytoplasmic free Ca2+ concentration by 75%, and the cytoplasmic free Ca2+ concentration response to BLX-1002 is also significantly suppressed
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
inhibits AMPK in a dose dependent manner. Suppresses AMPK activity during the early phase of adipogenic differentiation, which indicates that suppressed activation of AMPK may inhibit the mitotic clonal expansion process of preadipocytes. Levels of phosphorylated AMPKalpha and total AMPKalpha are not affected by 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, inhibits AMPK, whereby restores acid secretion
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
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
compound C
-
i.e. AMPKi or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a specific inhibitor of AMPK, largely impairs the activation of p38 MAPK upon UV radiation
compound C
(6-[4-(2-piperidin-1-yl-ethoxy)-phenyl])-3-pyridin-4-yl-pyrazolo[1,5-a]pyrimidine, a selective inhibitor, inhibition of the AMP-activated protein kinase alpha2 subunit kinase domain. Compound C binding dramatically alters the conformation of the activation loop, which adopts an intermediate conformation between DFG-out and DFG-in. The induced fit forms a compound-C binding pocket composed of the N-lobe, the C-lobe and the hinge of the kinase domain. The pocket partially overlaps with the putative ATP-binding pocket. Binding structure analysis, overview
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a specific inhibitor of AMPK
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
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
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a specific inhibitor of AMPK
glucocorticoid
-
treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
-
glucocorticoid
-
treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
-
additional information
-
genetic inhibition of LKB1 ablates statin-induced AMPK activation in endothelial cells
-
additional information
-
hypoxia decreases the expression level of AMPK beta1 isozyme by about 50%
-
additional information
-
insulin-resistance caused by high levels of D-glucose in the cell decreases the enzyme activity
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
-
additional information
-
physiological effects of AMPK activation and inhibition, mechanism, overview
-
additional information
-
activation of p38 in response to UV or H2O2 is inhibited in AMPKalpha siRNA-treated HaCaT cells, EGFR inhibitor PD 153035 and AG 1478 inhibit UV-induced AMPK and LKB1 activation
-
additional information
-
when glycogen becomes depleted, the glycogen-bound pool of AMPK becomes inhibited due to binding to alpha1-6-linked branch points exposed by the action of phosphorylase and/or debranching enzyme
-
additional information
-
protein phosphatase 2A (PP2A) and protein phosphatase 2C (PP2C) inactivate the active and phosphorylated form of AMPK in cell-free assays. Dephosphorylation of AMPK by PP2Calpha is inhibited by 5'-AMP
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additional information
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SOCS3, an inhibitor of leptin-STAT3 signalling, inhibits leptin activation of AMPK in primary myotubes
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additional information
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overexpression of reactive oxygen species scavenger catalase prevents hypoxia-induced AMPK activation
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additional information
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a significant reduction in AMPK activation and downstream acetyl-CoA carboxylase activation in response to viral Tat protein treatment. Knockdown of SIRT1 by siRNA potentiates Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation. Knockdown of AMPK by siRNA potentiates Tat-induced HIV-1 transactivation
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additional information
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activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
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additional information
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contraction in skeletal muscle in adenylate kinase null mice reduces AMPK activation due to lack of conversion of ADP to AMP
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additional information
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AMPK phosphorylation is significantly reduced in ob/ob mouse hearts compared with lean, wild-type controls and the reduction in active phosphorylated AMPKalpha is associated with an increase in protein phosphatase 2C (PP2C)
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additional information
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UCH-L3 is involved in a cell-autonomous down-regulation of AMPK activity
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additional information
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osteoclasts and macrophages generated from AMPK beta1-/- mice display no detectable AMPK activity
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additional information
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re-feeding after fasting inhibits AMPK activity in multiple hypothalamic regions. Diet-induced obesity mice have suppressed AMPK activity in the paraventricular nucleus of the hypothalamus, AMPK is suppressed to the level in leptin-treated chow-fed mice, and there is no further effect of leptin. In mice, diet-induced obesity alters the effect of leptin on AMPK activity not only in the hypothalamus, but also in the skeletal muscle. Adiponectin-deficient mice show decreased AMPK phosphorylation in the arcuate nucleus. In leptin-over-expressing transgenic mice on a high fat diet, muscle AMPK phosphorylation and acetyl-CoA carboxylase phosphorylation are reduced compared with standard diet leptin-over-expressing transgenic mice and are comparable to high fat diet-non-transgenic mice. Leptin i.c.v., in addition to transgenic hyperleptinaemia, is not able to restore the impaired AMPK signalling because of the induced generalised leptin resistance
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additional information
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in neurodegeneration model in which apoptotic neurodegeneration of neonatal mouse brains is induced by ethanol, AMPK activity is attenuated
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additional information
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no inhibition by adenosine-5'-pentaphospho-5'-adenosine
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additional information
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complex formation between isozyme alpha1 and NDPK-H1 inhibits the AMPK activity, inhibition by NDPK is reduced by addition of ADP or GTP, overview
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additional information
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prosurvival effects of rapamycin are consistent with mTOR inhibition being a critical downstream mediator of AMPK in persistent low oxygen
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additional information
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activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
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additional information
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inhibition or downregulation of AMPK via adenoviral delivery of dominant-negative AMPK-alpha prevents CO2-induced Na,K-ATPase endocytosis
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additional information
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AMPK phosphorylation is significantly reduced in Zucker diabetic fa/fa rats compared with lean, wild-type controls and the reduction in active phosphorylated AMPKalpha is associated with an increase in protein phosphatase 2C (PP2C). AMPK activity is reduced in aortic endothelium or skeletal muscle of obese rats compared with lean animals. Possibility that chronic exposure of cells to fatty acids may inhibit AMPK activation. Feeding of a high fat diet significantly decreases AMPK in the liver and muscles
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additional information
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lower basal AMPK activity in paraventricular nucleus may be due to effects of hyperinsulinaemia and/or hyperglycaemia, which suppress AMPK activity in multiple hypothalamic nuclei
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additional information
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autoinhibition of AMPK by the autoinhibitory domain. The autoinhibitory domain in the holoenzyme has a bona fide inhibiting role in the rate of phosphoryl transfer (kcat) as it does in the catalytic kinase domain/autoinhibitory domain fragments
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additional information
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kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 210
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additional information
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kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 189
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additional information
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dynamical mechanism of autoinhibition of AMP-activated protein kinase, molecular dynamics simulations and modelling, overview. Conformational switch model involving the movement of the kinase domain between an inactive unphosphorylated open state and an active or semi-active phosphorylated closed state, mediated by the autoinhibitory domain (AID). AID inhibits the catalytic function by restraining the kinase domain into an unproductive open conformation, thereby limiting local structural rearrangements, while mutations that disrupt the interactions between the kinase domain and AID allow for both the local structural rearrangement and global interlobe conformational transition. The AID also greatly impacts the structuring and mobility of the activation loop. Binding of AMP to the gamma-subunit changes the interactions between the AID and kinase domain to remove the inhibitory effect of AID to allow the interlobe conformational transition to the closed state. The unphosphorylated KD-AID fragment from Schizosaccharomycespombe (PDB ID 3H4J) is used as a model of the inactive-open state because of its open interlobe conformation, while the phosphorylated kinase domain fragment from Saccharomyces cerevisiae (PDB ID 3DAE) is used as the active-closed state reference, in accord with the experimental structural and mutagenesis analysis. AID inhibits catalytic function by restraining kinase domain to an inactive-open state
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(23E)-cucurbita-5,23,25-triene-3beta,7beta-diol
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CH10, triterpene from the stem of bitter melon Momordica charantia, leads to the activation of AMPK in cells, overcomes insulin resistance
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
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activates AMPK, phosphorylation of AMPK-Thr172 is increased 2.8fold in the degenerated midbrain by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-intoxication. AMPK activation is stimulated in the substantia nigra of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-intoxicated mice
1-methyl-4-phenylpyridinium
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activates AMPK in SH-SY5Y cells. Increases phosphorylation level at Thr172 in the active site of AMPKalpha. AMPK is activated during the progression of cell death mediated by 1-methyl-4-pyridinium
2-deoxyglucose
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blocks glucose utilization and increases the intracellular AMP concentration, activation is suppressed by compound C
24-hydroxyursolic acid
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from the leaves of Diospyros kaki, strongly activates AMPK, inhibits cell proliferation
3beta,25-dihydroxy-7beta-methoxycucurbita-5,23(E)-diene
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CH63, triterpene from the stem of bitter melon Momordica charantia, leads to the activation of AMPK in cells, overcomes insulin resistance
3beta,7beta,25-trihydroxycucurbita-5,23(E)-dien-19-al
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CH93, triterpene from the stem of bitter melon Momordica charantia, leads to the activation of AMPK in cells, overcomes insulin resistance
5-aminoimidazole-4-carboxamide ribonucleotide
Q13131 AND Q9Y478 AND P54619
i.e. AICAR, activation of AMPK in isolated perfused proximal renal tubules by AICAR
5-aminoimidazole-4-carboxamide-1-beta-D-riboside
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AICAR, activates AMPK, whereby significantly reduces secretagogue-induced acid secretion
A23187
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0.01 mM significantly enhances the phosphorylation of AMPK-Thr172 in BAEC. Either STO-609 (0.001 mM) or BAPTA-AM (0.02 mM), significantly suppresses calcium inophore A23187-enhanced phosphorylation in BAEC
A769662
Q13131 AND P54646
A769662 selectively activates beta1-containing AMPK isoforms
alpha,beta-methylene-ADP
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allosteric activator, can replace ADP, with 66% efficiency with bovine serum albumin as substrate
BLX-1002
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has no affinity to peroxisome proliferator-activated receptors (PPAR), stimulation of beta-cells with BLX-1002 induces activation of AMPK at high glucose. BLX-1002 selectively potentiates insulin secretion induced by high glucose in normal and diabetic islets in a PI3K-dependent manner. This effect is associated with an increased cytoplasmic free Ca2+ concentration mediated through Ca2+ mobilization, and an enhanced activation of AMPK
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BLX-1015
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0.01 mM significantly enhances AMPK phosphorylation, to an extent similar to that of BLX-1002. Potentiates pioglitazone-, but not fenofibrate-induced insulin secretion
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calyculin A
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stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
cantharidin
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stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
Colchicine
at low concentration (10 nM) promotes phosphorylation of AMPKalpha and macrophage M2 polarisation and reduces activation of caspase-1 and release of IL-1beta and CXCL1 by monosodium urate crystals in BMDMs in vitro. Activation of AMPK is induced by certain drugs already in the clinic for arthritis and other diseases (e.g. methotrexate, high-dose aspirin, metformin) and by other agents, including the selective and direct activator A-769661
compound C
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inhibits AMPK and phase II, but not phase I, of hypoxic pulmonary vasoconstriction
corticosterone
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counteracts inhibiting effect of sucrose and increases hypothalamic AMPK activity to levels comparable with saline-drinking animals
dexamethasone
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induces increase in AMPK in primary rat hypothalamic cell cultures, suggesting a direct effect of glucocorticoids on AMPK activity
Diethylamine NONOate
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nitric oxide donor, stimulates rapid and transient AMPK phosphorylation in INS832/13 cells and islets
hydrogen peroxide
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sublethal oxidative stress inhibits retinal pigment epithelium cell phagocytosis and activates AMPK. 0.5 mM hydrogen peroxide dramatically activates AMPKalpha, reaches the peak within 15 min, and declines 1 h later. Thr172 phosphorylation of catalytic subunit AMPKalpha is required for AMPKalpha activation
IFNgamma
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activates AMPK by phosphorylation of Thr172, independent of intracellular energy (ATP) levels. Phosphatidylinositol 3'-kinase inhibition by LY294002 partially prevents IFNgamma-induced activation of AMPK
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Insulin
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insulin-induced hypoglycaemia in rats increases AMPK phosphorylation and alpha2AMPK activity in the arcuate nucleus/dorso-mediobasal hypothalamus and paraventricular nucleus
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Mito-TEMPOL
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mitochondria-targeting superoxide dismutase mimetic, 0.01 mM markedly attenuates statin-enhanced phosphorylation of both AMPK-Thr172 and acetyl-CoA carboxylase-Ser79
MT-II
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melanocortin 4 receptor agonist, significantly augments AMPK and acetyl-CoA carboxylase phosphorylation, MT-II is a potent AMPK activator in muscle, even in mice on a high fat diet
nitric oxide
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AMPK is transiently activated by nitric oxide in insulinoma cells and rat islets following interleukin-1 treatment or by the exogenous addition of nitric oxide
O2
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hypoxia leads to time-dependent AMPK activation in ATII cells. Maximal activation of AMPK after 10 min of 1.5% O2 exposure, whereas 3% O2 activates AMPK in a similar but slower manner. AMPK levels return to the baseline after 30 min of hypoxia exposure. Hypoxia-generated mitochondrial reactive oxygen species leads to the activation of the AMPK alpha1 isoform at Thr172. Hypoxia fails to activate AMPK in mitochondrion-deficient rho0-A549 cells
okadaic acid
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stimulation of activating AMPK phosphorylation at Thr172, activation is antagonized by naringin
PKC-zeta
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is required for statin-induced LKB1 nucleus export and AMPK activation in HUVEC cells
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puerarin
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stimulates AMPK, puerarin down-regulated MDR1 expression via nuclear factor kappa-B and cAMP-responsive element transcriptional activity-dependent up-regulation of AMPK in MCF-7/adr cells
tautomycin
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stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
vascular endothelial growth factor
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activates AMPK in endothelial progenitor cells by phosphorylation at Ser172
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(+)-simvastatin
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0.05 mM increases phosphorylation of AMPK at Thr172 by 2.6fold and acetyl-CoA carboxylase at Ser79 in BAEC. Ser428 phosphorylation of LKB1 is essential for statin-induced AMPK activation. Statin-induced AMPK activation in BAEC is independent of CaMKKbeta. Activation of AMPK by statin Is O2- or ONOO- dependent
(+)-simvastatin
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LKB1 is required for statin-dependent AMPK activation. Transfection of LKB1-expressing plasmid is required for statin-induced AMPK activation in A-549 and HeLa S3 cell lines deficient in endogenous LKB1
(+)-simvastatin
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in vivo administration of statin increases 3-nitrotyrosine and the phosphorylation of AMPK and acetyl-CoA carboxylase in wild-type mice but not in mice deficient in endothelial nitric-oxide synthase. PKC-zeta-dependent AMPK activation. In vivo transfection of PKC-zeta-specific small interfering RNA in mice significantly attenuates statin-enhanced phosphorylation of AMPK-Thr172, acetyl-CoA carboxylase-Ser79, and LKB1-Ser428
5'-AMP
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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
5'-AMP
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up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5'-AMP
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up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5'-AMP
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5'-AMP
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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
5'-AMP
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up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside
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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
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside
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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
5-aminoimidazole-4-carboxamide ribonucleoside
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AICAR, has a proapoptotic effect in neuroblastoma cells. AICAR does not significantly change AMPK activity after prolonged exposure (48 h), when its apoptotic effect becomes evident
5-aminoimidazole-4-carboxamide ribonucleoside
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AICAR, AMPK activator, inhibits Tat-induced HIV-1 transactivation
5-aminoimidazole-4-carboxamide ribonucleoside
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AICAR, a potent activator of AMPK. If treated with small to moderate concentrations, embryonic hippocampal neurons cultured in conditions of glucose deprivation have improved survival
5-aminoimidazole-4-carboxamide riboside
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AICAR, increases phosphorylation of alpha1 AMPK, resulting in inactivation of ACCalpha in MAC-T cells
5-aminoimidazole-4-carboxamide riboside
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AICAR, activates AMPK, whereby increasing the rate of fatty acid oxidation in isolated human muscle strips and cultured human skeletal muscle cells. In isolated human muscle strips, AICAR induces glucose uptake, that is associated with increased translocation of the glucose transporter, GLUT4, to the plasma membrane
5-aminoimidazole-4-carboxamide riboside
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AICAR, its activation of AMPK is abolished by preincubation with dipyridamole or 5-iodotubercidin
5-aminoimidazole-4-carboxamide riboside
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AICAR, stimulates site 2 phosphorylation
5-aminoimidazole-4-carboxamide riboside
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AICAR is able to reverse both the inhibitory effect on pAMPK and the C75-induced anorexia
5-aminoimidazole-4-carboxamide riboside