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Information on EC 2.7.11.31 - [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase
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2.7.11.31 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinaseIUBMB Comments
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) . Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase . GTP can act instead of ATP
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Word Map
- 2.7.11.31
- insulin
- rapamycin
- metformin
- peroxisome
- mtor
-
proliferator-activated
- obesity
- carboxylase
- aicar
- acetyl-coa
- adipocytes
- cardiac
- triglyceride
- adiponectin
-
high-fat
- glycogen
- sterol
- mellitus
-
obese
- sirt1
- hypothalamic
-
antidiabetic
-
p-ampk
-
ampk-dependent
-
diet-induced
-
element-binding
- carnitine
- sirtuins
- 5-aminoimidazole-4-carboxamide
-
anti-obesity
-
hfd-induced
-
heterotrimeric
-
ampk-mediated
-
insulin-stimulated
-
phospho-ampk
-
glut-4
- ampkalpha
- protein-1c
- epitrochlearis
- drug development
-
adipor1
- coactivator-1
-
metformin-induced
- camkk
- srebp-1c
- 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside
-
palmitoyltransferase-1
- industry
-
insulin-independent
-
transporter-4
- medicine
- pharmacology
- dorsomorphin
-
energy-sensing
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
adenosine monophosphate-activated protein kinase, 5'-amp-activated protein kinase, snf1 kinase, prkaa1, adenosine 5'-monophosphate-activated protein kinase, reductase kinase, aak-2, amp-activated protein kinase alpha, ampkgamma, 5-amp-activated protein kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-AMP-activated protein kinase catalytic subunit alpha-1
adenosine monophosphate-activated protein kinase
AMP-activated protein kinase
AMPK
AMPKalpha
Snf1
Snf1 kinase
SNF1-interacting protein 1
SNF1-interacting protein 2
SNF1-interacting protein 3
SNF4
additional information
-
AMPK is a member of the serine/threonin protein kinases, as well as of a metabolite-sensing kinase family
AMP-activated protein kinase
-
-
AMP-activated protein kinase
-
-
AMP-activated protein kinase
-
-
AMPK
-
-
AMPK
-
-
AMPK
-
-
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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
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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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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 + 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 + cytoplasmic malate dehydrogenase
ADP + phosphorylated cytoplasmic malate dehydrogenase
-
-
?
ATP + dephospho-alpha,beta-tubulin
ADP + [alpha,beta-tubulin] phosphate
-
relative kinase activity high MW-kinase 15%
-
?
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
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; Q9Y478; P54619
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131; Q9Y478; 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 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 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
-
?
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NATURAL SUBSTRATE
NATURAL 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 + 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; Q9Y478; 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
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
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
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
?
-
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
?
-
-
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 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 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
ATP
-
-
662296, 663969, 665496, 690657, 690725, 691704, 692001, 692091, 692365, 693032, 693151, 693205, 693207, 693328, 694825, 701572
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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+
-
activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
Ca2+
-
increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview
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+
-
-
Mg2+
-
requirement, actual substrate: MgATP2-
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INHIBITOR
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
-
additional information
-
SOCS3, an inhibitor of leptin-STAT3 signalling, inhibits leptin activation of AMPK in primary myotubes
-
additional information
-
overexpression of reactive oxygen species scavenger catalase prevents hypoxia-induced AMPK activation
-
additional information
-
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
-
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
-
contraction in skeletal muscle in adenylate kinase null mice reduces AMPK activation due to lack of conversion of ADP to AMP
-
additional information
-
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)
-
additional information
-
UCH-L3 is involved in a cell-autonomous down-regulation of AMPK activity
-
additional information
-
osteoclasts and macrophages generated from AMPK beta1-/- mice display no detectable AMPK activity
-
additional information
-
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
-
additional information
-
in neurodegeneration model in which apoptotic neurodegeneration of neonatal mouse brains is induced by ethanol, AMPK activity is attenuated
-
additional information
-
no inhibition by adenosine-5'-pentaphospho-5'-adenosine
-
additional information
-
complex formation between isozyme alpha1 and NDPK-H1 inhibits the AMPK activity, inhibition by NDPK is reduced by addition of ADP or GTP, overview
-
additional information
-
prosurvival effects of rapamycin are consistent with mTOR inhibition being a critical downstream mediator of AMPK in persistent low oxygen
-
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
-
inhibition or downregulation of AMPK via adenoviral delivery of dominant-negative AMPK-alpha prevents CO2-induced Na,K-ATPase endocytosis
-
additional information
-
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
-
additional information
-
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
-
additional information
-
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
-
additional information
-
kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 210
-
additional information
-
kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 189
-
additional information
-
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
-
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
-
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
-
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
-
blocks glucose utilization and increases the intracellular AMP concentration, activation is suppressed by compound C
24-hydroxyursolic acid
-
from the leaves of Diospyros kaki, strongly activates AMPK, inhibits cell proliferation
3beta,25-dihydroxy-7beta-methoxycucurbita-5,23(E)-diene
-
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
-
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; Q9Y478; P54619
i.e. AICAR, activation of AMPK in isolated perfused proximal renal tubules by AICAR
5-aminoimidazole-4-carboxamide-1-beta-D-riboside
-
AICAR, activates AMPK, whereby significantly reduces secretagogue-induced acid secretion
A23187
-
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
A769662 selectively activates beta1-containing AMPK isoforms
alpha,beta-methylene-ADP
-
allosteric activator, can replace ADP, with 66% efficiency with bovine serum albumin as substrate
BLX-1002
-
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
-
BLX-1015
-
0.01 mM significantly enhances AMPK phosphorylation, to an extent similar to that of BLX-1002. Potentiates pioglitazone-, but not fenofibrate-induced insulin secretion
-
calyculin A
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
cantharidin
-
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
-
inhibits AMPK and phase II, but not phase I, of hypoxic pulmonary vasoconstriction
corticosterone
-
counteracts inhibiting effect of sucrose and increases hypothalamic AMPK activity to levels comparable with saline-drinking animals
dexamethasone
-
induces increase in AMPK in primary rat hypothalamic cell cultures, suggesting a direct effect of glucocorticoids on AMPK activity
Diethylamine NONOate
-
nitric oxide donor, stimulates rapid and transient AMPK phosphorylation in INS832/13 cells and islets
hydrogen peroxide
-
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
-
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
-
Insulin
-
insulin-induced hypoglycaemia in rats increases AMPK phosphorylation and alpha2AMPK activity in the arcuate nucleus/dorso-mediobasal hypothalamus and paraventricular nucleus
-
Mito-TEMPOL
-
mitochondria-targeting superoxide dismutase mimetic, 0.01 mM markedly attenuates statin-enhanced phosphorylation of both AMPK-Thr172 and acetyl-CoA carboxylase-Ser79
MT-II
-
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
-
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
-
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
-
stimulation of activating AMPK phosphorylation at Thr172, activation is antagonized by naringin
PKC-zeta
-
is required for statin-induced LKB1 nucleus export and AMPK activation in HUVEC cells
-
puerarin
-
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
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
vascular endothelial growth factor
-
activates AMPK in endothelial progenitor cells by phosphorylation at Ser172
-
(+)-simvastatin
-
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
-
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
-
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
-
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
-
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
-
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
-
-
5'-AMP
-
the gamma subunit of AMPK contains adenine nucleotide binding sites that facilitate the direct interaction of AMP with the AMPK heterotrimer. AMP regulates the activity of AMPK via the inhibition of AMPK dephosphorylation by protein phosphatases
5'-AMP
-
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
-
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
-
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
-
AICAR, AMPK activator, inhibits Tat-induced HIV-1 transactivation
5-aminoimidazole-4-carboxamide ribonucleoside
-
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
-
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
-
AICAR, increases phosphorylation of alpha1 AMPK, resulting in inactivation of ACCalpha in MAC-T cells
5-aminoimidazole-4-carboxamide riboside
-
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
-
AICAR, its activation of AMPK is abolished by preincubation with dipyridamole or 5-iodotubercidin
5-aminoimidazole-4-carboxamide riboside
-
AICAR is able to reverse both the inhibitory effect on pAMPK and the C75-induced anorexia
5-aminoimidazole-4-carboxamide riboside
-
AICAR, stimulates site 2 phosphorylation
5-aminoimidazole-4-carboxamide riboside
-
stimulation of activating AMPK phosphorylation at Thr172
5-aminoimidazole-4-carboxamide riboside
-
i.e. AICAR, a specific AMPK activator
5-aminoimidazole-4-carboxamide riboside
-
AICAR, activation of the alpha2 isoform of AMPK in response to treatment with the AMPK activator AICAR, is much greater in the glycogen-depleted state
5-aminoimidazole-4-carboxamide riboside
-
AICAR, in perfused hindlimb, AICAR induces glucose uptake, that is associated with increased translocation of the glucose transporter, GLUT4, to the plasma membrane. Reduces insulin-stimulated glycogen synthase activity in isolated skeletal muscle. Diminishes ectopic lipid deposition in liver and muscle of Zucker diabetic fatty rats and slows the progression to type 2 diabetes in these animals
5-aminoimidazole-4-carboxamide riboside
-
AICAR, increases phosphorylation of acetyl-CoA carboxylase and AMPK in INS832/13 cells
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, increase in cytosolic Ca2+ activity by Ca2+ ionophore ionomycin triggeres eryptosis, an effect blunted by the AMPK activator 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside at 1 mM
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, increases AMPK activity
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
i.e. AICAR, activates AMPK activity with substrate CREB about 3fold, and AMPK signaling in muscles but not in LBK1-KO mice, overview
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
activates AMPK in BMMs and RAW264.7 cells. While 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside greatly stimulates osteoclast formation, it acts through an AMPK-independent mechanism
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, activating phosphorylation of alphaAMPK T172 in response to AICAR increases normally in muscle from obese mice fed a high-fat diet
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, activates AMPK, wherby altering the expression of a variety of genes, including those for uncoupling protein (UCP)-3 and GLUT-4 in muscle, and fatty acid synthase and phosphoenolpyruvate carboxykinase in hepatocytes
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, chronic AMPK activation with AICAR decreases blood pressure in rats displaying features of the insulin resistance syndrome
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, a potent agonist of AMPK, activates AMPK activation by p38 MAPK, AICAR must be phosphorylated itself to ZMP by adenosine kinases in order to activate AMPK
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, activates AMPK and increases PGC-1alpha expression
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, an AMP-activated protein kinase specific activator
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, decreases class III PI3-kinase binding to beclin-1, and this effect counteracts and reverses the known positive effect of AMPK activity on autophagy, and AICAR inhibits the proteasomal degradation of proteins in lysosomes by an AMPK-dependent mechanism, but inhibits autophagy by an AMPK-independent mechanism
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, the activation of AMPK negatively modulates the activated phenotype of hepatic stellate cells, AMPKactivation does not reduce PDGF-dependent activation of extracellular signal-regulated kinase, ERK, or Akt, but blocks in cell cycle progression, physiological effects of AMPK activation and inhibition, mechanism, overview
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, activates the phosphorylation of peptide QKFQRELSTKWVLN 4fold, kinetics, overview
A-769662
-
small molecule direct activator of AMPK, increases glucose uptake in both L6 myotubes and primary myotubes
A-769662
-
small molecule direct activator of AMPK, treatment of ob/ob mice for 5 days decreases plasma glucose and triglyceride concentrations, lowers hepatic triglyceride content and reduces expression of gluconeogenesis genes in the liver
A-769662
a selective pharmacological activator of AMPK. A-769662 promotes AMPK-dependent macrophage anti-inflammatory M2 polarisation and inhibits NLRP3 gene expression, activation of caspase-1 and IL-1beta
A-769662
-
activates the liver enzyme, binds to the enzyme, acts allosterically
A-769662
-
small molecule direct activator of AMPK, reduces fatty acid synthesis in primary hepatocytes
adiponectin
-
activation of AMPK, which is mediated via cell surface receptor AdipoR1
-
AMP
P54646; O43741; Q9UGI9
an allosteric activator for AMPK heterotrimeric complex (alpha2beta2gamma3)
AMP
phosphorylation of the activation-loop threonine (Thr172 of alpha2) or allosteric modulation by AMP binding is essential for AMPK activation
AMP
the alpha2-subunit-containing enzyme complexes are more readily activated by AMP than alpha1-complexes
AMP
-
-
AMP
-
wild-type is activated about 2fold in the presence of 0.2 mM. The catalytic activity and substrate binding affinity of AMPK are separately regulated by AMP binding and the assembly of beta- and gamma-subunits onto the alpha-subunit
Ca2+/calmodulin-dependent protein kinase kinase
-
i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview
-
Ca2+/calmodulin-dependent protein kinase kinase
-
i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview
-
Calmodulin
-
AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
Calmodulin
-
activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
dinitrophenol
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
dinitrophenol
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
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
-
interleukin-6
-
activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK
interleukin-6
-
activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK
interleukin-6
-
directly activates AMPK in vivo and in vitro. Activates AMPK in skeletal muscle by increasing the concentration of cAMP and the AMP:ATP ratio. AMPK activation coincides temporally with a nearly 3fold increase in the AMP:ATP ratio in the extensor digitorum longus
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
leptin
-
has a tissue-specific effect on AMPK. In the skeletal muscle, it stimulates AMPK activity
-
metformin
-
AMPK mediates the prevention of progression of heart failure by metformin. Protective effects of AMPK activation by metformin on cardiovascular disease
metformin
-
increases the activating phosphorylation of the enzyme at Thr172 of the alpha-subunit by 3.6fold
metformin
-
i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview
metformin
-
improves cardiac structure and function, which is associated with increases in AMPK and endothelial nitric oxide synthase phosphorylation, as well as increased peroxisome proliferator-activated receptor-gamma coactivator (PGC)-1alpha expression in cardiac myocytes. Cardioprotective effects of metformin are ablated in mice lacking functional AMPK or nitric oxide synthase
metformin
-
significantly increases AMPK activity in the aortas and hearts of wild-type mice but not those of eNOS-/-, although eNOS-/- mice express AMPK
metformin
-
stimulates AMPK, does not induce any significant change in glucose-stimulated insulin secretion
metformin
-
co-administration of dexamethasone and metformin decreases insulin-stimulated glucose uptake compared with metformin alone
metformin
-
i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview
pioglitazone
-
i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in humans via activation of AMPK in skeletal muscle
pioglitazone
-
i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle
Reductase kinase kinase
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activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
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Reductase kinase kinase
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EC 2.7.1.110, activation in presence of MgATP2-
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Reductase kinase kinase
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activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
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resveratrol
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reverses Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation, inhibits Tat-induced HIV-1 transactivation
resveratrol
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increases the phosphorylation status of AMPK in wild-type MEFs. Effect of resveratrol on AMPK is mediated via LKB1
resveratrol
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resveratrol exerts anti-hypertrophic effects by activating AMPK via LKB1 and inhibiting Akt, thus suppressing protein synthesis and gene transcription. Level of phosphorylated AMPK is significantly increased in resveratrol-treated cardiac myocytes in the absence or presence of phenylephrine
rosiglitazone
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i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in humans via activation of AMPK in skeletal muscle
rosiglitazone
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stimulates an increase in the ADP/ATP ratio and AMPK activity essentially involving LKB1 and leading to activation of nitric oxide synthesis in human