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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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- 2.7.11.31
- metformin
- rapamycin
- peroxisome
- obesity
- aicar
- mtor
- carboxylase
-
proliferator-activated
- acetyl-coa
- endothelial
- cardiac
-
high-fat
- triglyceride
- adipocytes
- adiponectin
- glycogen
- agonist
- mellitus
-
obese
- sterol
- hypothalamic
- steatosis
- sirt1
-
antidiabetic
-
ampk-dependent
-
diet-induced
- sirtuins
- leptin
-
p-ampk
- 5-aminoimidazole-4-carboxamide
-
lipogenesis
-
insulin-stimulated
-
ampk-mediated
- myotubes
-
element-binding
-
hfd-induced
-
anti-obesity
- srebp-1c
- ulk1
- camkks
-
adipor1
- coactivator-1
-
palmitoyltransferase-1
- dorsomorphin
- drug development
-
phospho-ampk
- epitrochlearis
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metformin-induced
- phenformin
-
energy-sensing
-
insulin-independent
- medicine
- industry
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
adenosine monophosphate-activated protein kinase, amp-activated kinase, 5'-amp-activated protein kinase, prkaa1, snf1 kinase, adenosine 5'-monophosphate-activated protein kinase, ampkalpha1, reductase kinase, aak-2, ampk alpha2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
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3-hydroxy-3-methylglutaryl-CoA reductase kinase
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5'-AMP-activated protein kinase catalytic subunit alpha-1
adenosine monophosphate-activated protein kinase
AMP-activated protein kinase
AMP-activated protein kinase alpha
AMPK
AMPKalpha
AMPKalpha1
AMPKalpha2
beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
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-
-
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EC 2.7.1.109
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formerly
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hydroxymethylglutaryl coenzyme A reductase kinase
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hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating)
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reductase kinase
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Snf1
Snf1 kinase
SNF1-interacting protein 1
SNF1-interacting protein 2
SNF1-interacting protein 3
SNF4
[hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase
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additional information
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AMPK is a member of the serine/threonin protein kinases, as well as of a metabolite-sensing kinase family
AMP-activated protein kinase
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AMP-activated protein kinase
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
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AMP-activated protein kinase
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AMP-activated protein kinase
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AMP-activated protein kinase
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AMPK
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AMPK
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
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AMPK
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AMPK
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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
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphotransferase
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) [5]. Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase [7]. GTP can act instead of ATP [4]
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CAS REGISTRY NUMBER
COMMENTARY
172522-01-9
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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
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relative kinase activity for low-MW kinase 7%, high MW-kinase 87%
-
-
?
ATP + heavy meromyosin
ADP + [heavy meromyosin] phosphate
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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
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relative kinase activity for low-MW kinase 38%, high MW-kinase 159%
-
-
?
ATP + histone VIIIS
ADP + [histone VIIIS] phosphate
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relative kinase activity for low-MW kinase 65%, high MW-kinase 141%
-
-
?
ATP + HMKSAMSGLHLVKRR
ADP + ?
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synthetic SAMS-containing peptide as substrate
-
-
?
ATP + JAK1
ADP + phosphorylated JAK1
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phosphorylation at Ser515 and Ser518
-
-
?
ATP + MAP-2
ADP + MAP-2 phosphate
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relative kinase activity for low-MW kinase 14%, high MW-kinase 566%
-
-
?
ATP + myelin basic protein
ADP + [myelin basic protein] phosphate
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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
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relative kinase activity for low-MW kinase 4%, high MW-kinase 27%
-
-
?
ATP + neurofilament triplet L protein
ADP + [neurofilament triplet L protein]phosphate
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-
-
-
?
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
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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
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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
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rabbit muscle glycogen synthase
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
-
-
-
-
?
ATP + RNA-binding protein HUR
ADP + ?
-
inhibits the protein by phosphorylation
-
-
?
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
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phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + phospho-[acetyl-CoA carboxylase]
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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
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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
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phosphorylation at about 90% the rate of ATP
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-
?
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
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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
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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
-
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 phosphorylation 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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + JAK1
ADP + phosphorylated JAK1
-
phosphorylation at Ser515 and Ser518
-
-
?
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 + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
-
-
-
-
?
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
-
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
-
-
-
?
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 phosphorylation 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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
(5Z)-2-[(3-hydroxyphenyl)amino]-5-(1H-indol-3-ylmethylidene)-1,3-thiazol-4(5H)-one
-
-
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
-
-
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
potent and selective inhibitor; potent and selective inhibitor
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
-
-
(Z)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxylic acid
78% inhibition at 0.01 mM; 85% inhibition at 0.01 mM
(Z)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-N-propyl-1H-pyrrole-3-carboxamide
30% inhibition at 0.01 mM; 48% inhibition at 0.01 mM
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
-
-
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((6-methyl-2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
88% inhibition at 0.01 mM; 89% inhibition at 0.01 mM
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
potent and selective inhibitor; potent and selective inhibitor
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
-
(Z)-N-(2-(diethylamino)ethyl)-5-((5-fluoro-1-methyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
17% inhibition at 0.01 mM; 40% inhibition at 0.01 mM
(Z)-N-(2-(diethylamino)ethyl)-5-((6-ethyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
90% inhibition at 0.01 mM
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-5-((6-isopropyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
69% inhibition at 0.01 mM; 70% inhibition at 0.01 mM
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
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
-
N-(2-[[2-(1H-indol-3-yl)ethyl]amino]-2-oxoethyl)-3-phenyl-2,1-benzoxazole-5-carboxamide
-
-
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
sunitinib, subunit AMPKalpha1 shows about 50% inhibition at 100 nM; sunitinib, subunit AMPKalpha2 shows 46% inhibition at 100 nM
nicotinamide
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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
sunitinib
subunit AMPKalpha1 shows about 50% inhibition at 100 nM; subunit AMPKalpha2 shows 46% inhibition at 100 nM
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
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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
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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
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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
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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
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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
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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
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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
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compound C
compound C
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i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
compound C
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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
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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
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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
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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
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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
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i.e. 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-yl-pyrazolo[1,5-a]pyrimidine
glucocorticoid
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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
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glucocorticoid
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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
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metformin
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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
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
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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
(5S)-3-[(13S)-13-hydroxy-14-(2-{[(2S)-2-hydroxydodecyl]oxy}ethoxy)tetradecyl]-5-methylfuran-2(5H)-one
-
i.e. AA005
-
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-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
GINST
-
a hydrolyzed ginseng extract, phosphorylation of AMPKalpha increases 2.5fold by GINST after 360 min of treatment
-
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
N-(3-hydroxyphenyl)adenosine
-
activates the enzyme with 1.4fold maximal activity at 0.001 mM
-
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
-
[([5-(5-oxo-4,5-dihydro-1,2-oxazol-3-yl)furan-2-yl]phosphoryl)bis(oxy)methylene]bis(2-methylpropanoate)
-
i.e. C13
(+)-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 ribonucleotide
Q13131; Q9Y478; P54619
i.e. AICAR, activation of AMPK in isolated perfused proximal renal tubules by AICAR
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
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
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
-
activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
-
Reductase kinase kinase
-
EC 2.7.1.110, activation in presence of MgATP2-
-
Reductase kinase kinase
-
activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
-
resveratrol
-
reverses Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation, inhibits Tat-induced HIV-1 transactivation
resveratrol
-
increases the phosphorylation status of AMPK in wild-type MEFs. Effect of resveratrol on AMPK is mediated via LKB1
resveratrol
-
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
-
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
-
stimulates an increase in the ADP/ATP ratio and AMPK activity essentially involving LKB1 and leading to activation of nitric oxide synthesis in human aortic endothelial cells, the stimulation of AMPK and NO synthesis by rosiglitazone is unaffected by the peroxisome proliferator-activated receptor-gamma inhibitor GW9662 or by STO-609, overview
rosiglitazone
-
i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle
rotenone
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
rotenone
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
additional information
-
decreases in energy availability or rises in intracellular Ca2+ most likely activates AMPK in MAC-T cell
-
additional information
-
AAK-2 is phosphorylated at Thr243 and activated in response to paraquat treatment, the phosphorylation depends on PAR-4, the Caenorhabditis elegans LKB1 homologue
-
additional information
-
AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals
-
additional information
the region flanking the regulatory T172 site of AMPKalpha subunit is phosphorylated by an upstream AMPKK. AMPK is activated during temperature stress. AMPK activity remains constant between 12 and 18°C, but increases up to 9.1fold between 18 and 30°C. Total AMPK protein expression levels do not vary significantly over this temperature range. Prolonged exposure for up to 6 h to the sublethal temperature of 26°C leads to a constant elevation of AMPK activity. Increase in AMPK activity above 18°C coincides with the decrease in reaction time
-
additional information
the region flanking the regulatory T172 site of AMPKalpha subunit is phosphorylated by an upstream AMPKK. AMPK is activated during temperature stress. AMPK activity remains constant between 12 and 18°C, but increases up to 9.1fold between 18 and 30°C. Total AMPK protein expression levels do not vary significantly over this temperature range. Prolonged exposure for up to 6 h to the sublethal temperature of 26°C leads to a constant elevation of AMPK activity. Increase in AMPK activity above 18°C coincides with the decrease in reaction time
-
additional information
-
AMPK activity increases 5.5fold in liver during hypoxic exposure accompanied by a change in the AMP/ATP ratio, but not in muscle, brain, heart, or gill, overview
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
-
additional information
-
activation of AMPK requires phosphorylation at Thr172 by an AMPK kinases, e.g. LKB1 and Ca2+/calmodulin-dependent kinase kinase, CaMKK
-
additional information
-
AMPKalpha needs to be activated by phosphorylation on Thr172
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
the enzyme is activated by phosphorylation at Thr172 in the alpha subunit activation T-loop
-
additional information
-
UV and H2O2 induce AMPK activation through Thr172 phosphorylation, UV and H2O2 also phosphorylate LKB1, an upstream signal of AMPK, in an epidermal growth factor receptor-dependent manner, overview. SB203580, a p38 inhibitor, does not affect AMPK activation
-
additional information
-
activation of the alpha2 isoform of AMPK in response to exercise in human muscle, is much greater in the glycogen-depleted state. In humans with McArdle's disease (glycogen storage disease V), the activation of AMPK-alpha2 in response to a moderate level of exercise (which is all these subjects can tolerate) is significantly higher than in the controls
-
additional information
-
in healthy humans, an acute bout of exercise activates AMPK in an isoform and intensity-dependent manner
-
additional information
-
LKB1, a serine-threonine kinase of 433 amino acids, which contains both a kinase domain and a nuclear localization signal in its N-terminal region, phosphorylates the T-loop of AMPK
-
additional information
all three nucleotides AMP, ADP and ATP can bind to sites 1 and 3 with similar affinities. Phosphorylation of Thr172/Thr174 of the alpha subunit activates the enzyme isozymes
-
additional information
Q13131; Q9Y478; P54619
ischemia stimulates the AMP-activated protein kinase (AMPK)
-
additional information
P54646; O43741; Q9UGI9
small molecule activator thienopyridone A-769662 has no ativating effect on AMPK heterotrimeric complex (alpha2beta2gamma3)
-
additional information
the enzyme is activated under circumstances with an increased cellular AMP:ATP ratio, such as metabolic stresses that inhibit ATP production (hypoxia, glucose deprivation, metabolic inhibitors etc.) and those that stimulate ATP consumption (exercise, cell growth and division etc.). Activation-loop conformation, overview
-
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
-
phosphorylation at Thr172 activates the enzyme, the phosphorylation is activated by 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
T cell receptor stimulation activates AMPK due to energy needs in case of cell division having regulatory function, overview. AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
-
additional information
-
ADP does not directly control AMPK activity but can do so indirectly through the adenylate kinase equilibrium with AMP and ATP
-
additional information
-
in skeletal muscle of Uchl3-/- mice fed a normal chow diet, phosphorylated AMPK is significantly up-regulated, which indicates an increased activation of AMPK, in any feeding state. No AMPK activation in other major metabolic tissues, such as liver and white adipose tissue. Embryonic fibroblasts derived from Uchl3-/- mice also show increased activation of AMPK, indicating that UCH-L3 is involved in a cell-autonomous down-regulation of AMPK
-
additional information
-
methanol extracts from the fruit, seed, or stem of bitter melon Momordica charantia all contain components efficacious in improving glucose uptake of insulin-resistant cells involving activation of AMPK
-
additional information
-
mice subjected to moderate diet restriction (60% of the requirement) are characterized by AMPK activation. Drastic diet restriction (40% of the requirement) leads to further elevation in AMPK activity
-
additional information
-
overexpression of GDE in cells causes increased phosphorylation of the AMPK alpha subunit at Thr-172 and its consequent activation
-
additional information
phosphorylation on Thr172 and activation of AMPKalpha subunit
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
activated by phosphorylation by upstream protein kinases AMPKK and CaMKIK
-
additional information
-
AMPK can also be activated by hyperosmotic stress
-
additional information
-
stimulation by protein phosphatase-inhibitory toxins
-
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
-
AMPKalpha needs to be activated by phosphorylation on Thr172. Reactive oxygen species contribute to AMPK activation, mechanism, overview
-
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
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme, copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
additional information
-
the enzyme is activated by phosphorylation at Thr172
-
additional information
-
AMPK may be sensitive to the lipid status of a cell and activation may be influenced by intracellular fatty acid availability independent of cellular AMP levels
-
additional information
-
diabetic rats treated with cilostazol, a selective inhibitor of phosphodiesterase 3, exhibit normalization of endothelial function that is linked to AMPK activation producing increased endothelial nitric oxide synthase activity and NO production. In the ischemic heart, both catalytic alpha1-isoform and alpha2-isoform of AMPK containing regulatory gamma1-isoform or gamma2-isoform are activated
-
additional information
-
elevated phosphorylation of AMPK and R2-GABAB in the hippocampus of a rat ischemic in vivo model
-
additional information
-
inhibition of intracellular glucose utilisation through the administration of 2-deoxyglucose increases hypothalamic AMPK activity and food intake. Diabetic rats have enhanced AMPK activity, despite their high glucose levels, which should suppress hypothalamic AMPK. Thyroid hormones stimulate AMPK and acetyl-CoA carboxylase expression in skeletal muscle. 1 h of strenuous exercise in rats does not elicit significant changes in hypothalamic AMPK activity despite an increase in plasma ghrelin
-
additional information
-
adenosine (0.0001-0.5 mM) has no direct stimulating effect on enzyme activity
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
-
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
-
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
-
protein kinases Elm1, Pak1 and Tos3 phosphorylate and activate SNF1
-
additional information
-
hydrophobic contacts between the kinase domain and the autoinhibitory domain have a predominant role in controlling the conformational change between low- and high activity forms of AMPK
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02667
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.03207
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.03731
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.08003
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.1076
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.1214
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
additional information
additional information
glucosyl-beta-cyclodextrin binding kinetics, association and dissociation, and thermodynamics
-
additional information
additional information
glucosyl-beta-cyclodextrin binding kinetics, association and dissociation, and thermodynamics
-
additional information
additional information
theMichaelis-Menten enzyme kinetics and allosteric modulation of six recombinant AMPK isoforms, alpha1beta1gamma1, alpha1beta2gamma1, alpha1beta2gamma3, alpha2beta1gamma1, alpha2beta2gamma,1 and alpha2beta2gamma3 using known activators, A769662 and AMP. The alpha1-containing complexes exhibit higher specific activities and lower Km values for peptide substrate biotin-GGHMRSAMSGLHLVKRR-NH2 (SAMS) compared with alpha2-complexes. Binding affinities of AMP, ADP and ATP using surface plasmon resonance techniques, all three nucleotides AMP, ADP and ATP can bind to sites 1 and 3 with similar affinities, allosteric regulation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000111 - 0.000418
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
-
0.000108 - 0.000184
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000101 - 0.000139
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000324 - 0.000164
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000607 - 0.000107
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000162 - 0.000093
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
-
0.0000825 - 0.000208
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000651 - 0.000217
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000836 - 0.000205
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
-
0.0000885 - 0.000246
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
0.000154 - 0.0021
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000205 - 0.000173
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000966 - 0.000296
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
0.000348
(Z)-N-(2-(diethylamino)ethyl)-5-((6-ethyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000494 - 0.00024
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000504 - 0.000136
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000614 - 0.00018
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000141 - 0.000393
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000386 - 0.000152
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000748 - 0.000221
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000158 - 0.00617
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000111
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000418
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.000108
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000184
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000101
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000139
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000324
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000164
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000607
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000107
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000162
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000093
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.0000825
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000208
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000651
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000217
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000836
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000205
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.0000885
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000246
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000154
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.0021
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000205
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000173
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000966
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000296
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.0000494
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.00024
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000504
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000136
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000614
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.00018
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000141
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000393
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000386
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000152
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000748
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000221
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000158
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.00617
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
5.9
subunit AMPK-beta, calculated from amino acid sequence
6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma3, calculated from amino acid sequence
6.1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma1, calculated from amino acid sequence
6.3
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKbeta1b, calculated from amino acid sequence
6.6
7.1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKalpha1, calculated from amino acid sequence
7.3
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKalpha2, calculated from amino acid sequence
8.6
subunit AMPK-alpha, calculated from amino acid sequence
9
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma2b, calculated from amino acid sequence
5.6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKbeta1a, calculated from amino acid sequence
5.6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKbeta2, calculated from amino acid sequence
6.6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma2a, calculated from amino acid sequence
6.6
subunit AMPK-gamma, calculated from amino acid sequence
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two alpha, two beta, and five gamma gene orthologues encoding the subunit variants
-
-
brenda
-
644981, 644984, 662296, 665496, 690657, 690725, 691704, 692001, 692091, 692365, 692554, 693032, 693151, 693205, 693207, 693328, 694825, 701571, 701572, 701573, 702079, 703102, 703277, 703348, 703612, 704431, 704459, 704545, 705267, 705694, 705799, 705939, 706364, 706902
-
-
brenda
-
644989, 665636, 687732, 690346, 691621, 692365, 693047, 694183, 701571, 701572, 701573, 701620, 702510, 703277, 703348, 703612, 703617, 704122, 704433, 704450, 705267, 705939, 706085
-
-
brenda
-
286565, 491403, 644952, 644953, 644954, 644956, 644957, 644959, 644961, 644963, 644964, 644971, 644972, 644973, 644976, 644977, 644978, 644979, 644983, 644988, 663952, 665636, 684366, 690726, 691556, 691704, 692365, 692682, 693207, 701572, 701573, 703277, 703348, 704433, 705267, 705884, 705939, 761360, 761734, 762101
-
-
brenda
male sprague-dawley rats
-
-
brenda
beta subunit Gal83, equivalent to subunit beta 3
UniProt
brenda
beta subunit Sip1, equivalent to subunit beta 1
UniProt
brenda
beta subunit Sip2, equivalent to subunit beta 2
UniProt
brenda
beta subunit Gal83, equivalent to subunit beta 3
UniProt
brenda
beta subunit Sip1, equivalent to subunit beta 1
UniProt
brenda
beta subunit Sip2, equivalent to subunit beta 2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
selective expression of the AMPKalpha1 catalytic subunit in lymphoid cells
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
additional information
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
-
visceral adipose tissue, the predominant AMPK subunit in adipose tissue is AMPKalpha1
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKbeta1a
brenda
-
AMPK is widely expressed throughout the brain, including several areas controlling food intake and neuroendocrine function
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKbeta1b
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKbeta2
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma1
brenda
of female and male oysters, expression of AMP-activated protein kinase (AMPK) subunits during gametogenesis in the gonad, overview. AMPK beta transcripts in the gonad at different reproductive stages decrease from stage 1 to 3
brenda
of female and male oysters, expression of AMP-activated protein kinase (AMPK) subunits during gametogenesis in the gonad, overview. AMPK gamma transcripts amounts in the gonad at different reproductive stages are quit constant
brenda
of female and male oysters, expression of AMP-activated protein kinase (AMPK) subunits during gametogenesis in the gonad, overview. Subunit AMPK alpha mRNA levels are more abundant in males at the first stage of gametogenesis, when mitotic activity and the differentiation of germinal cells occur, and are always more abundant in males than in females. AMPKalpha Thr172 phosphorylation appears to be almost totally inhibited in mature female gonads at stage 3, at the time when accumulation of reserves in oocytes is promoted, while it remains at a high level in mature spermatozoa. Truncated (45-kDa) and entire (62-kDa) AMPK alpha proteins are detected in gonads of both males and females at all reproductive stages. In both males and females, AMPK alpha truncated protein is detected at a very low level, and its amount does not vary significantly during reproduction, while the entire AMPK alpha protein is detected at a high level, and its amount varies significantly during reproduction. AMPK alpha transcripts in the gonad at different reproductive stages decreases from stage 1 to 3
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKalpha2
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma2a
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma3
brenda
-
HeLa cells stably expressing wild type LKB1 or a kinase-inactive mutant LKB1
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKalpha1
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
-
the hibernating 13-lined ground squirrel actively increases its fat stores in the liver during the summer, and this is associated with relatively low enzyme (total AMP-activated protein kinase, P-AMPK) activity. During hibernation fat synthesis is turned off while fat oxidation is increased and P-AMPK is activated, especially during the IBA. During torpor activity of P-AMPK declines
brenda
-
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286565, 490912, 491403, 644952, 644953, 644954, 644955, 644956, 644957, 644959, 644961, 644964, 644967, 644971, 644972, 644973, 644978, 644980, 644983, 644988, 663969, 684366, 691132, 691704, 692682, 693207, 701571, 704936
brenda
-
AMPK activity in the liver is significantly higher in corticosterone-treated rats compared with the untreated ones
brenda
-
AMPKalpha1beta1gamma1 is the main isoform expressed in liver
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
brenda
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma2b
brenda
-
different isozymes in muscles by different combinations of subunits, i.e. alpha1/beta2/gamma1, alpha2/beta2/gamma1, and alpha2/beta2/gamma3, overview
brenda
P54646; O43741; Q9UGI9
in human skeletal muscle, the alpha2beta2gamma3 complexes constitutes the majority of AMPK heterotrimers
brenda
-
gastrocnemius, tibialis anterior, heart, and epitrochlearis muscle
brenda
-
-
brenda
additional information
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AMPKalpha1 and AMPKbeta1 genes are ubiquitously expressed in goldfish tissues, AMPKalpha1a is most highly expressed in brain, kidney, and intestine, AMPKalpha1b in brain, kideny, and gill, AMPKbeta1 is most highly expressed in brain
brenda
additional information
activity status of AMPK in the gonadic tissue of male and female oysters reared under natural conditions
brenda
additional information
activity status of AMPK in the gonadic tissue of male and female oysters reared under natural conditions
brenda
additional information
activity status of AMPK in the gonadic tissue of male and female oysters reared under natural conditions
brenda
additional information
the alpha2 isoform is abundant in cardiac and skeletal muscle
brenda
additional information
-
present in BMM cells. Osteoclasts and macrophages lack AMPK beta2 subunit expression
brenda
additional information
-
present in BMM cells. Osteoclasts and macrophages lack AMPK beta2 subunit expression
-
brenda
additional information
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
brenda
additional information
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
brenda
additional information
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
brenda
additional information
-
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
brenda
additional information
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cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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at prophase, P-AMPKalpha-Thr172 associates with the two asters of microtubules that begin to nucleate from mature centrosomes. Overlapping localization of P-AMPKalpha-Thr172 with the mitotic centrosomal Aurora-A kinase on the microtubules near the spindle poles in metaphase and in early anaphase. Localization of P-AMPKalpha-Thr172 at the central spindle and midbody persists during the furrowing process and at the completion of telophase. P-AMPKalpha-Thr172 localization at centrosomes requires dynamic microtubules
brenda
-
AMPK alpha and beta subunits are located both in the cytosol (associated to the rough endoplasmic reticulum) and in close association with rosettes of glycogen particles. Labeling for the alpha(1) and alpha(2) subunits of AMPK is about 2fold greater over glycogen than over cytosol, whereas labeling for beta(1) is 8fold higher over the glycogen particles than over the cytosol. The beta(1) subunits are located at the periphery of the glycogen rosettes
-
brenda
additional information
-
-
brenda
-
AMPK alpha and beta subunits are located both in the cytosol (associated to the rough endoplasmic reticulum) and in close association with rosettes of glycogen particles. Labeling for the alpha(1) and alpha(2) subunits of AMPK is about 2fold greater over glycogen than over cytosol, whereas labeling for beta(1) is 8fold higher over the glycogen particles than over the cytosol
brenda
-
-
-
brenda
beta subunit Gal83-containing isozyme after activation by alkaline stress, when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
brenda
-
beta subunit Gal83-containing isozyme after activation by alkaline stress, when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
-
brenda
additional information
-
differential localization patterns of AMPKalpha 1 and AMPKalpha2
-
brenda
additional information
-
differential localization patterns of AMPKalpha 1 and AMPKalpha2
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
evolution
the AMPK beta-subunit CBM has a beta-sandwich fold with the conserved residues Trp100, Lys126 and Trp133 (residue numbers according to beta1-CBM), classifying it under the CBM48 family
evolution
the genes encoding the three subunits of AMPK are highly conserved in eukaryotic species for which complete genome sequences are available, including vertebrates, invertebrates, plants, fungi, and protozoa
evolution
-
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
-
malfunction
-
Agouti-related peptide alpha2 AMPK-KO mice show decreased body weight even though there are no changes in food intake or energy expenditure and, the difference in body weight is lost when the animals are fed a high fat diet. Pro-opiomelanocortin alpha2 AMPK-KO animals show increased body weight and adiposity, which is further enhanced by a high fat diet
malfunction
-
AMPK gamma2 mutations are associated with hypertrophic cardiomyopathy
malfunction
-
germline deletion of either AMPK beta1 or beta2 subunit isoforms results in reduced trabecular bone density and mass, but without effects on osteoclast or osteoblast numbers, as compared to wild-type littermate controls
malfunction
-
in the liver from beta1 knockout mice the gamma1 subunit is present but alpha1 and alpha2 are degraded
malfunction
-
mice deficient in AMPKalpha-2 have smaller infarct volumes after middle cerebral artery occlusion, whereas AMPKalpha-1 deficiency has no effect compared to wild-type
malfunction
-
mice lacking either the alpha1 or alpha2 AMPK catalytic subunits demonstrate that AMPK is required for the effect of AICAR on glucose uptake. Transgenic mice expressing an inactive form of AMPK alpha2 subunit specifically in skeletal muscle develop impaired whole-body glucose tolerance and iInsulin resistance in skeletal muscle, particularly when fed a high-fat diet
malfunction
-
mutations in the gamma2 and gamma3 subunits result in glycogen storage disease
malfunction
-
mutations in the gamma2 and gamma3 subunits result in glycogen storage disease. Ten point mutations in gamma2 are associated with a glycogen storage cardiomyopathy and ventricular pre-excitation
malfunction
deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2
malfunction
knockout of AMPKalpha1 enhances, and, conversely, activator A-769662 inhibits monosodium urate crystal-induced inflammatory responses including IL-1beta and CXCL1 release in vitro and in vivo
malfunction
stabilization of MAPO1 occurs in AMPKalpha-knockdown cells even without N-methyl-N-nitrosourea treatment. Knockdown of the Flcn and Ampkalpha genes by specific siRNAs significantly suppresses an apoptotic response to N-methyl-N-nitrosourea
malfunction
the absence of functional AMPK may consequently cause a failure of distinct signaling pathways in red bood cells
malfunction
-
enzyme ablation increases Zika virus replication and reduces innate antiviral responses
malfunction
Mus musculus C57BL/6/129
-
knockout of AMPKalpha1 enhances, and, conversely, activator A-769662 inhibits monosodium urate crystal-induced inflammatory responses including IL-1beta and CXCL1 release in vitro and in vivo
-
malfunction
-
germline deletion of either AMPK beta1 or beta2 subunit isoforms results in reduced trabecular bone density and mass, but without effects on osteoclast or osteoblast numbers, as compared to wild-type littermate controls
-
malfunction
-
deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2
-
metabolism
-
active AMPK promotes the functional recovery of beta-cell oxidative metabolism and abrogates the induction of pathways that mediate cell death such as caspase-3 activation following exposure to nitric oxide
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a metabolic energy regulator that can switch acid secretion off as cellular ATP levels fall. Secretagogue-induced acid secretion can be significantly reduced with AMPK activation and restored with its deactivation
metabolism
-
plays an important role in the regulation of both lipid and glucose metabolism. Direct link between AMPK activation and fatty acid metabolism. Has the potential of ameliorating insulin resistance and improving glucose homeostasis. A gain-of-function mutation in the gene encoding AMPK gamma3-subunit is reported to confer beneficial effects on muscle fuel metabolism
metabolism
-
SNF1 protein kinase cascade, sharing functional similarities with mammalian AMPK, which plays an important role in adapting the unicellular eukaryote to glucose starvation
physiological function
-
activation of AMPK alpha is necessary for hypoxia-induced AMPK-PKCzeta binding in alveolar epithelial cells. Overexpression of a dominant-negative AMPK alpha subunit construct prevents hypoxia-induced endocytosis of Na,K-ATPase, hypoxia-induced PKCzeta translocation to the plasma membrane and phosphorylation at Thr410
physiological function
-
activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease
physiological function
-
activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease. Overexpression of AMPK increases cell viability after exposure to 1-methyl-4-pyridinium in SH-SY5Y cells
physiological function
-
AMPK activation alters the expression of a variety of genes, including phosphoenolpyruvate carboxykinase in hepatocytes. Reduced AMPK activation may play an important role in the lipid accumulation and genesis of endothelial dysfunction in obese rats. Endothelial AMPK activity may inhibit glycerol-3-phosphate acyltransferase, required for de novo synthesis of diacylglycerol
physiological function
-
AMPK activation and subsequent increases in fatty acid beta-oxidation in skeletal muscle leads to increased energy expenditure in Uchl3-/- mice
physiological function
-
AMPK activation dramatically decreases de novo fatty acid synthesis and inactivates ACCalpha. AMPK activation modifies lipogenic gene expression including fatty acid synthase, glycerol-3-phosphate acyltransferase, and fatty acid binding protein-3. AMPK is able to inhibit fatty acid synthesis, an energy consuming process, in response to decreases in energy supply
physiological function
-
AMPK activation during oxidative stress may switch retinal pigment epithelium cells to a self-protected status. Alpha2 but not alpha1 AMPK is involved in retinal pigment epithelium cell phagocytosis and activation of alpha2 AMPK contributes to the inhibition of retinal pigment epithelium cell phagocytosis by oxidative stress
physiological function
-
AMPK activation induces vasodilatation and blood flow regulation in wild-type mice and this effect is abolished in AMPKalpha1 knockout mice. Chronic activation of AMPK in vivo attenuates ROS-mediated c-Jun N-terminal kinase activation and endothelial dysfunction in response to angiotensin II, which is abrogated in mice lacking the endothelial isoform of AMPKalpha1 or peroxisome proliferator gamma coactivator-1alpha, a target of AMPK that controls mitochondrial biogenesis. AMPK-deficient mice demonstrate impairment in postischemic fatty acid oxidation. In the setting of systolic pressure overload, left ventricular hypertrophy ensues and AMPKalpha2 knockout mice exhibit significantly increased overload-induced ventricular hypertrophy and decreased left ventricular ejection fraction. Isolated hearts of AMPK-deleted mice show increased apoptosis and dysfunction after ischemia/reperfusion. Role of AMPK in regulation of apoptosis that is an important mechanism of heart failure
physiological function
-
AMPK activation inhibits endothelial apoptosis in cultured cells. AMPK activation suppresses the basal and angiotensin II-enhanced superoxide anions in BAEC
physiological function
-
AMPK activation inhibits ICAM-1 mediated migration of lymphocytes across primary microvascular endothelial cells
physiological function
-
AMPK activation inhibits TNFa-stimulated leukocyte adhesion to aortic endothelial cells and ICAM-1 mediated migration of lymphocytes across primary microvascular endothelial cells
physiological function
-
AMPK is required for proper cell division and faithful chromosomal segregation during mitosis. Active form of the alpha-catalytic AMPK subunit (P-AMPKalpha-Thr172), but not its total form (AMPKalpha), transiently associates with several mitotic structures including centrosomes, spindle poles, the central spindle midzone and the midbody throughout all of the mitotic stages and cytokinesis in human cancer-derived epithelial cells
physiological function
-
AMPK is required to maintain normal bone density, but not through bone cell differentiation, and does not mediate powerful osteolytic effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
physiological function
-
AMPK is responsible for phosphorylation of site 2 in vivo. Both basal and 5-aminoimidazole-4-carboxamide riboside (AICAR)-stimulated site 2 phosphorylation is greatly reduced in muscles of AMPK-alpha2 knockout mice
physiological function
-
AMPK may play an important role in protecting endothelial cells against adverse effects of sustained hyperglycaemia, such as alterations in fatty acid metabolism, impaired Akt activation by insulin, increased caspase 3 activity and apoptosis. It may modulate endothelial cell energy supply. The AMPK-acetyl CoA carboxylase-malonyl CoA-carnitine palmitoyl-transferase 1 mechanism for regulating long-chain fatty acid oxidation, similar to that of muscle, operates in the endothelial cell and is regulated by AMPK under physiological conditions. One way to deal with endothelial lipotoxicity is to promote free fatty acid oxidation and ameliorate lipid accumulation in endothelial cells, which can be achieved by activating endothelial AMPK. AMPK inhibits fatty acid-induced increases in NF-kappaB transactivation in cultured human umbilical vein endothelial cells
physiological function
-
AMPK mediates cold-induced resistance to anorexigenic signalling in the hypothalamus. Activation of AMPK can contribute to hyperphagia. Inhibition of AMPK inhibits the hypoglycaemia-induced increase in the counter-regulatory hormones glucagon, corticosterone and catecholamines, causing a severe and prolonged hypoglycaemia
physiological function
-
critical role of AMPK in the survival of circulating erythrocytes. As compared with erythrocytes from wild-type littermates (ampk+/+), erythrocytes from AMPKalpha1-deficient mice (ampk-/-) are significantly more susceptible to the eryptotic effect of energy depletion. The ampk-/- mice are anemic despite excessive reticulocytosis, and they suffer from severe splenomegaly
physiological function
-
overexpression or ablation of the AMPK gamma3 subunit does not appear to play a critical role in defining mitochondrial content in resting skeletal muscle. Skeletal muscle mitochondrial content is unaltered in AMPK gamma3-/- mice
physiological function
-
plays a crucial role in carbon catabolite repression in yeast. cRKIN1 gene product from rye can rescue SNF1 mutation
physiological function
-
role for AMPK, in concert with other signals induced by IFNgamma, in mediating reduced epithelial barrier function in a cell model of chronic intestinal inflammation
physiological function
-
role of AMPK is that it monitors cellular energy status by sensing the relative cellular concentrations of AMP and ATP. The beta-subunits of AMPK contain a glycogen-binding domain, which is a regulatory domain that allows AMPK to act as a sensor of the status of cellular reserves of energy in the form of glycogen. The pool of AMPK that is bound to the glycogen particle is in an active state when glycogen particles are fully synthesized, causing phosphorylation of glycogen synthase at site 2 and providing a feedback inhibition of further extension of the outer chains of glycogen
physiological function
-
transgenic littermates overexpressing an alpha2AMPK kinase-dead (KD) have reduced skeletal muscle alpha2AMPK activity (50% in gastrocnemius and more than 80% in soleus and extensor digitorum longus) and acetyl-CoA carboxylase-2 Ser228 phosphorylation (90% in gastrocnemius). Obesity in response to high-fat feeding is not associated with impaired AMPK actions, obesity-induced lipid accumulation and insulin resistance are not exacerbated in AMPK KD mice
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor to maintain energy balance at both the cellular and the whole-body levels. The enzyme is activated under circumstances with an increased cellular AMP:ATP ratio, such as metabolic stresses that inhibit ATP production (hypoxia, glucose deprivation, metabolic inhibitors etc.) and those that stimulate ATP consumption (exercise, cell growth and division etc.)
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that is essential in regulating energy metabolism in all eukaryotic cells
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that serves as a pleotropic regulator of whole body energy homoeostasis. The enzyme is allosterically regulated, kinetic analysis, overview. Binding of activator AMP to the gamma-subunit allows a small regulatory segment of the alpha-subunit (alpha2 residues 365-371) called the alpha-hook or alpha-RIM2 to directly interact with bound AMP and create an allosteric conformational change at the catalytic active site. As a consequence, the phosphorylated alpha-Thr172/174 can be protected from dephosphorylation by phosphatases and sustain its kinase activity for an extended period
physiological function
P54646; O43741; Q9UGI9
AMP-activated protein kinase (AMPK) is an energy-sensing serine/threonine protein kinase that plays a central role in whole-body energy homeostasis. The muscle-specific AMPK heterotrimeric complex (alpha2beta2gamma3) is involved in glucose and fat metabolism in skeletal muscle
physiological function
AMP-activated protein kinase (AMPK) is metabolic biosensor with anti-inflammatory activities. Gout is commonly associated with excesses in soluble urate and in nutrition, both of which suppress tissue AMPK activity. Gout is driven by macrophage-mediated inflammation transduced partly by NLRP3 inflammasome activation and interleukin-1beta release. AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages. Activated AMPK is anti-inflammatory partly through inhibition of NF-kappaB
physiological function
-
AMP-activated protein kinase (AMPK) maintains the balance between ATP production and energy consumption in eukaryotic cells by responding to the rise of intracellular AMP
physiological function
AMPK is a cellular energy sensor that negatively regulates cell growth and proliferation. MAPO1, identified as a component involved in the induction of apoptosis, is stabilized by interaction with AMP-activated protein kinase (AMPK) and folliculin (FLCN). AMPK is activated during the process of O6-methylguanine-induced apoptosis and this activation is dependent on MAPO1 and folliculin. It is likely that the kinase activity of AMPK is involved in the degradation of MAPO1
physiological function
AMPK is a metabolic stress-sensing kinase with important functions for red blood cell survival. Identification of putative AMPK targets in hemoglobin-depleted lysates of erythrocytes, including metabolic enzymes, cytoskeletal proteins and enzymes involved in the oxidative stress response, cloning and recombinant expression. AMPK aids the function of red blood cells
physiological function
Q13131; Q9Y478; P54619
ischemia stimulates the AMP-activated protein kinase (AMPK), a serine/threonine kinase, sensing energy depletion and stimulating several cellular mechanisms to enhance energy production and to limit energy utilization. AMPK downregulates the epithelial Na+ channel ENaC mediated by the ubiquitin ligase Nedd4-2. AMPK regulates the heterotetrameric K+-channel KCNQ1/KCNE1. Wild-type and constitutively active AMPK significantly reduce KCNQ1/KCNE1-mediated currents and reduce KCNQ1 abundance in the cell membrane of transfected Xenopus laevis oocytes, overview. AMPK decreased the KCNQ1 protein abundance in the cell membrane via ubiquitin ligase Nedd4-2
physiological function
sex-specific regulation of AMP-activated protein kinase alpha in the Pacific oyster Crassostrea gigas. AMPKalpha activation might play a sex-dependent role in management of energy during gametogenesis in oyster
physiological function
sex-specific regulation of AMP-activated protein kinase in the Pacific oyster Crassostrea gigas
physiological function
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
physiological function
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2
physiological function
-
enzyme phosphorylation inhibits the activation of human hepatic stellate cell line LX-2. Enzyme activation in LX-2 cells inhibits autophagosome formation. Enzyme activation inhibits transforming growth factor-beta-induced intracellular lipid droplet depletion, which relies on increased autophagic flux, and finally inhibits transforming growth factor-beta-induced hepatic stellate cell activation
physiological function
-
intrinsic activation of the enzyme has functional protective effects in the reperfused atria when glucose is the only available energetic substrate whereas it is deleterious when palmitate is also available
physiological function
-
once activated, the enzyme suppresses the necessary enzymes involved in ATP-consuming anabolic pathways and enhances cellular ATP supply. Enzyme activation can facilitate bacterial eradication in sepsis and related inflammatory conditions associated with the inhibition of neutrophil activation and chemotaxis. The enzyme also inhibits nuclear factor-kappaB signaling and inflammation
physiological function
-
the enzyme couples inhibition of mitochondrial metabolism by hypoxia to acute hypoxic pulmonary vasoconstriction and progression of pulmonary hypertension. Inhibition of complex I of the mitochondrial electron transport chain activates the enzyme and inhibits Kv1.5 channels in pulmonary arterial myocytes. The enzyme is the primary mediator of reductions in Kv1.5 channels following inhibition of mitochondrial oxidative phosphorylation during hypoxia and by mitochondrial poisons
physiological function
-
the enzyme has an antiviral effect on Zika virus replication. The anti-Zika virus effect of enzyme signaling in endothelial cells is mediated by reduction of viral-induced glycolysis and enhanced innate antiviral responses
physiological function
Mus musculus C57BL/6/129
-
AMP-activated protein kinase (AMPK) is metabolic biosensor with anti-inflammatory activities. Gout is commonly associated with excesses in soluble urate and in nutrition, both of which suppress tissue AMPK activity. Gout is driven by macrophage-mediated inflammation transduced partly by NLRP3 inflammasome activation and interleukin-1beta release. AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages. Activated AMPK is anti-inflammatory partly through inhibition of NF-kappaB
-
physiological function
-
AMPK is required to maintain normal bone density, but not through bone cell differentiation, and does not mediate powerful osteolytic effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
physiological function
-
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
physiological function
-
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2
-
additional information
alpha1-subunit containing AMPK isoforms possess higher basal activity and are less sensitive to desphosphorylation by phosphatases compared with alpha2-subunit containing heterotrimers. The alpha2-subunit-containing complexes are more readily activated by AMP than alpha1-complexes. Enzymatic activity, phosphatase sensitivity and kinetics of alpha1- and alpha2-containing AMPK isoforms, differential effect of activators, overview
additional information
-
residues Glu42, Arg81, Asp156, and Phe175 of the isolated kinase domain fragment have greater conformational flexibility in the closed state, with the hinge residue Gly116 exhibiting two conformational basins in the closed state, and Gly115 already in an active-closed state conformation even when the interlobe conformation is open
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
-
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
the AMPK alpha2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the DFG-out conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter
additional information
-
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
-
Show AA Sequence and Transmembrane Helices (1596 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
155000
P54646; O43741; Q9UGI9
recombinant His-tagged full-length alpha2beta2gamma3 heterotrimeric AMPK complex, gel filtration
35000
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
36000
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
38000
58000
63000
38000
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
38000
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
63000
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
63000
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
trimer
additional information
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 29230, subunit AMPKbeta1b, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 29620, subunit AMPKbeta2, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 30410, subunit AMPKbeta1a, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 38260, subunit AMPKgamma3, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 39130, subunit AMPKgamma1, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 55530, subunit AMPKgamma2a, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 60380, subunit AMPKgamma2b, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 62290, subunit AMPKalpha2, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 64700, subunit AMPKalpha1, calculated from amino acid sequence
?
x * 37953, recombinant phosphorylated AMPK alpha1 subunit, mass spectrometry
?
x * 110700, subunit AMPK-gamma, calculated from amino acid sequence
?
x * 33000, subunit AMPK-beta, calculated from amino acid sequence
?
x * 58800, subunit AMPK-alpha, calculated from amino acid sequence
heterotrimer
AMPK is a heterotrimeric kinase composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma
heterotrimer
P54646; O43741; Q9UGI9
1 * 64000, recombinant His-tagged alpha2 subunit, + 1 * 54000, recombinant His-tagged beta2 subunit, + 1* 33000, recombinant His-tagged gamma3 subunit, SDS-PAGE
heterotrimer
AMPK exists as a heterotrimeric complex, composed of a catalytic subunit (alpha) and two regulatory subunits (beta and gamma), each present as multiple isoforms
heterotrimer
enzyme AMPK is a heterotrimeric protein complex composed of a catalytic subunit (alpha) and two regulatory subunits (beta and gamma)
heterotrimer
enzyme AMPK is composed of AMPKalpha, beta and gamma subunits
heterotrimer
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
heterotrimer
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
heterotrimer
AMPK is heterotrimer with alphabetagamma structure
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
alphabetagamma heterotrimer composed of different alpha, beta, and gamma subunit variants
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits, with multiple genes encoding each subunit in mammals, alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3
trimer
-
different heterotrimers resulting in different isozymes, the alphabetagamma composition can be formed by two different alpha subunit variants, two different beta and three different gamma subunits, overview
trimer
-
heterotrimeric AMPK consists of a catalytic alpha subunit, and regulatory beta and gamma subunits
trimer
-
in human skeletal muscle, the alpha2beta2gamma3 complexes constitute the majority of AMPK heterotrimers
trimer
-
alphabetagamma heterotrimer composed of different alpha, beta, and gamma subunit variants
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits, with multiple genes encoding each subunit in mammals, alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
a heterotrimeric enzyme with a catalytic alpha subunit, and regulatory beta and gamma subunits, of which exists different variants
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits, with multiple genes encoding each subunit in mammals, alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3
trimer
heterotrimer, complex structure determination and analysis by mass spectrometry, dynamic light and small-angle X-ray scattering and transmission electrom microscopy, modeling, overview
trimer
-
in rat skeletal muscle, the alpha2beta2gamma1 complexes constitute the majority of AMPK heterotrimers
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
additional information
-
heterotrimeric serine/threonine kinase consists of a catalytic alpha-subunit and 2 regulatory subunits beta and gamma, each subunit exists as multiple isoforms, alpha1, alpha2, beta1, beta2, gamma1, gamma2 and gamma3, giving 12 different possible combinantions of holoenzyme with different tissue distribution and subcellular localization
additional information
-
heterotrimeric serine/threonine kinase consists of a catalytic alpha-subunit and 2 regulatory subunits beta and gamma, each subunit exists as multiple isoforms, alpha1, alpha2, beta1, beta2, gamma1, gamma2 and gamma3, giving 12 different possible combinantions of holoenzyme with different tissue distribution and subcellular localization
additional information
-
AMPK consists of a catalytic alpha subunit and two non-catalytic subunits,beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers
additional information
-
several isoforms for each of the three AMPK subunits, including alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, AMPKalpha subunit possesses a highly conserved, N-terminal catalytic domain that contains the activating phosphorylation site Thr172, an autoinhibitory domain, and a C-terminus that contains the domains required for binding with the beta and gamma subunits, subunit structures, overview
additional information
P54646; O43741; Q9UGI9
AMPK is a heterotrimeric enzyme with a catalytic (alpha) subunit and two regulatory (beta and gamma) subunits
additional information
the AMPK alpha2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the DFG-out conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket. Three-dimensional structure analysis, overview. The kinase domain structures display the typical bilobal protein-kinase fold
additional information
-
the alpha1-subunit isoform accounts for 90% of the total AMPK in vascular smooth muscle
additional information
-
heterotrimeric serine/threonine kinase consists of a catalytic alpha-subunit and 2 regulatory subunits beta and gamma, each subunit exists as multiple isoforms, alpha1, alpha2, beta1, beta2, gamma1, gamma2 and gamma3, giving 12 different possible combinantions of holoenzyme with different tissue distribution and subcellular localization
additional information
-
AMPK consists of a catalytic alpha subunit and two non-catalytic subunits,beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers, beta1-Thr263 and beta1-Tyr267 are required for beta1gamma1 subunit association
additional information
-
several isoforms for each of the three AMPK subunits, including alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, AMPKalpha subunit possesses a highly conserved, N-terminal catalytic domain that contains the activating phosphorylation site Thr172, an autoinhibitory domain, and a C-terminus that contains the domains required for binding with the beta and gamma subunits, subunit structures, overview
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM). The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, determination of the NMR solution structure, structure analysis
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM). The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, determination of the NMR solution structure, structure analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
the subunit beta sequence contains an N-myristoylation site
phosphoprotein
phosphoprotein
-
AAK-2 is phosphorylated at Thr243 in response to paraquat treatment, the phosphorylation depends on PAR-4, the Caenorhabditis elegans LKB1 homologue
phosphoprotein
-
AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals
phosphoprotein
phosphorylation of the catalytic AMPK alpha protein at threonine 172
phosphoprotein
serine 108 and serine 182 phosphorylation sites in subunit beta
phosphoprotein
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
phosphoprotein
-
the enzyme is phosphorylated at Thr172 of its alpha-subunit, phosphorylation activates the enzyme, metformin increases the enzyme phosphorylation
phosphoprotein
-
8-chloro-cAMP and no 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside induce AMPK phosphorylation
phosphoprotein
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
phosphoprotein
-
activation of AMPK requires phosphorylation at Thr172 by an AMPK kinases, e.g. LKB1 and Ca2+/calmodulin-dependent kinase kinase, CaMKK
phosphoprotein
-
phosphorylation at alpha1-Thr172 by CaMKKbeta, and at alpha1-Ser485, beta1-Ser108, and beta1-Ser182 in Sf21 cells, determination of phosphorylation sites by mass spectrometry, phosphorylation also by LKB1, overview
phosphoprotein
-
phosphorylation of AMPK at Thr172 of the alpha-subunit inducd by 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
phosphoprotein
-
the enzyme is activated by phosphorylation at Thr172 in the alpha subunit activation T-loop
phosphoprotein
-
UV and H2O2 induce AMPK activation through Thr172 phosphorylation
phosphoprotein
activation of the enzyme by phosphorylation of Thr172 of the alpha subunit. Thr172 is the only site phosphorylated by its upstream kinase, liver kinase B1, and the phosphorylation dramatically increases the kinase activity of the catalytic domain/alpha-subunit. Phosphorylation of AMPK alpha1 on Thr172 by LKB1/Ste20-related adaptor (STRAD)/mouse protein 25(MO25) complex. Top-down mass spectrometric analysis, overview. Ser18 and Ser22 in the His-tag region as well as Thr196 (equivalent to Thr172 in the unmodified enzyme) in the sequence of the AMPK catalytic domain are the three phosphorylation sites
phosphoprotein
autophosphorylation of 5'-AMP-activated protein kinase catalytic subunit alpha-1
phosphoprotein
enzyme activation by phosphorylation on Thr172, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, ATM and TAK1 are AMPK kinases
phosphoprotein
phosphorylation of Thr172/Thr174 of the alpha subunit activates the enzyme isozymes
phosphoprotein
-
the enzyme can be activated by direct phosphorylation by the upstream kinase liver kinase B1 at the site of Thr172 on the alpha-subunit, or through indirect allosteric changes of the gamma-subunit, thereby regulating the phosphorylation state of the alpha-subunit
phosphoprotein
-
Zika virus infection results in a decrease in AMPKalpha phosphorylation at Thr172
phosphoprotein
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
phosphoprotein
-
phosphorylation at Thr172 activates the enzyme, the phosphorylation is activated by 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
phosphoprotein
phosphorylation on Thr172 and activation of AMPKalpha subunit
phosphoprotein
-
protein kinase B increases the phosphorylation of AMPKalpha1 subunit at Ser485/Ser491, which subsequently prevents the phosphorylation of the enzyme at Thr172 by liver kinase B1 and thus suppresses the activation of the enzyme
phosphoprotein
-
upstream kinases boost phosphorylation of the enzyme on threonine 172 at the alpha catalytic subunit for enzymatic activation
phosphoprotein
Mus musculus C57BL/6/129
-
phosphorylation on Thr172 and activation of AMPKalpha subunit
-
phosphoprotein
-
the enzyme is activated by phosphorylation at Thr172, which is inhibited by naringin
phosphoprotein
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
phosphoprotein
-
AMPK is activated by phosphorylation, induced e.g. by leptin
phosphoprotein
-
AMPKalpha needs to be activated by phosphorylation on Thr172
phosphoprotein
-
phosphorylation by CaMKKbeta and LKB1, determination of phosphorylation sites by mass spectrometry, overview
phosphoprotein
-
phosphorylation of AMPK at Thr172 of the alpha-subunit
phosphoprotein
when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
phosphoprotein
-
when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the inactive, apo-form of AMPK alpha2 subunit N-terminal kinase catalytic domain (KCD, residues 10-278 inclusive), shows that it adopts a canonical bilobal structure with the active site forming a cleft between the two lobes. The small N-terminal lobe (residues 1-97) is composed of a five-stranded beta-sheet (beta1-beta5), with an alpha-helix (termed the C-helix) positioned between strands beta3 and beta4 and lying to one side of the beta sheet. Glu-64 within the C-helix is important for aligning the phosphates of ATP in the correct orientation for catalysis. A Gly-X-Gly-X-X-Gly P-loop motif connecting strands beta1 and beta2 is evident in the structure. This interacts with the beta phosphate group of ATP when the active site is occupied. The larger C-terminal lobe is predominantly (63%) alpha-helical (alphaD-alphaI) and contains determinants and structural features that dictate protein substrate binding. The two lobes are connected via a short, flexible hinge region that allows rotation of the two lobes relative to each other
-
purified AMPK alpha2 subunit in apoform and in complex with compound C inhibitor, for the apoform: hanging-drop vapour diffusion method, mixing of 2.8 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 0.3 M NaCl, 10% glycerol, 2 mM DTT, 5 mM MgCl2, and 5 mM AMPPNP, with reservoir solution consisting of 0.1 M Tris-HCl pH 8.9, 15% 2-propanol, 0.1 M ammonium sulfate, and 16% PEG 4000, for the complexed form: sitting-drop vapour-diffusion method, mixing of 2.8 mg/mlprotien in 20 mM Tris-HCl, pH 8.5, 0.3 M NaCl, 10% glycerol, 2 mM DTT, 5 mM MgCl2, and 0.5 mM compound C, with reservoir solution consisting of 0.1 M Bis-Tris, pH 6.5, 1.5 M ammonium sulfate, and 0.1 M NaCl, 20°C, X-ray diffraction structure determination and analysis at 2.08-3.0 A resolution, molecular replacement, modelling, overview
crystal structure of AMPK beta1 subunit-carbohydrate-binding module in complex with the cyclic sugar beta-cyclodextrin shows that the domain consists of a beta-hairpin loop extending from a beta-sandwich containing two anti-parallel beta-sheets. The sugar ring is held in position by the beta-hairpin loop, which protrudes the ring with Leu-146 at its centre. Within the sugarbinding pocket an extensive network of hydrophobic stacking interactions, mediated by Trp100 and Trp133, and carbohydrate-protein hydrogen bonds are formed with five of the seven glucose units. Although Leu-146 is prominent in the beta7-beta8 hairpin and interacts extensively with beta-cyclodextrin, it is not essential for glycogen binding
-
purified subunit beta1 carbohydrate-binding module CBD in complex with glucosyl-beta-cyclodextrin, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 13 mg/ml protein in 20 mM HEPES, pH 7.0, and 6 mM gBCD, with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate, 25% w/v PEG 8000, and 0.1 M sodium acetate, pH 4.5, X-ray diffraction structure determination and analysis at 1.72 A resolution, molecular replacement
purified subunit beta2 carbohydrate-binding module, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 13 mg/ml protein in 20 mM HEPES, pH 7.0, with or without 6 mM glucosyl-beta-cyclodextrin, with 0.001 ml of reservoir solution, which contains for the unliganded enzyme 0.17 M ammonium sulfate, 15% v/v glycerol and 25.5% w/v PEG 4000, or contains 0.2 M lithium chloride, 20% w/v PEG 6000 and 0.1 M sodium HEPES, pH 7.0 for the complex with gBCD, X-ray diffraction structure determination and analysis at 1.6-2.0 A reolution, molecular replacement
crystals grown by mixing proteins with ammonium formate. Crystal structure of phosphorylated kinase domain, to 2.9 A resolution. Phosphorylated kinase domain displays a closed conformation
-
crystal structures for full-length Snf4. In the subunit crystal structure ADP can be co-crystallized and occupies site 2, the unoccupied site present in mammalian gamma1
-
crystals grown by mixing proteins with ammonium sulphate. Crystal structure of an unphosphorylated fragment of the AMPK alpha-subunit that contains both the catalytic kinase domain and an autoinhibitory domain, to 2.8 A resolution. The unphosphorylated kinase domain of catalytic kinase domain/autoinhibitory domain fragment adopts an open inactive conformation. Kinase domain/autoinhibitory domain is jammed into its active site, and the critical catalytic residues make several intra- and intermolecular contacts
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K45R
R225W
-
naturally occuring mutation of the gamma3 subunit, which leads to a 2fold increased AMPK activity, a 90% increase in skeletal muscle glycogen content and a 30% decrease in triglycerides
R70Q
T172D
R225Q
D157A
D329K
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
F300E
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
H150R
-
constitutively active AMPKgamma1 mutant, stimulates the concentration-dependent increase of substrate phosphorylation
I327D
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
K45R
-
dominant negative AMPKalpha2 mutant, results in a concentration-dependent inhibition in the phosphorylation of the AMPK substrate, inhibits endogenous AMPK activation. Inhibition of AMPK attenuates recovery of aconitase activity and promotes caspase-3 activation during recovery
L326D
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
N330A
-
catalytic kinase domain/autoinhibitory domain mutant, shows little or no effect on specific activity
R263A
-
catalytic kinase domain/autoinhibitory domain mutant, shows little or no effect on specific activity
V296D
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
Y267A
-
the mutation almost completely abrogates the beta1gamma1 interaction in comparison to wild type enzyme
Y267F
-
the mutation affects the beta1gamma1 interaction in comparison to wild type enzyme
Y267H
-
the mutation affects the beta1gamma1 interaction in comparison to wild type enzyme
Y267S
-
the mutation affects the beta1gamma1 interaction in comparison to wild type enzyme
H379A
site-directed mutagenesis, mutation of beta subunit Gal83 with little effect on Gal83 function
H380A
site-directed mutagenesis, mutation of beta subunit Sip2, mutation does not affect heterotrimer association
H384A
site-directed mutagenesis, mutation of beta subunit Gal83 causing a severe loss of function when assayed for growth on alternative carbon sources, the mutation does not affect heterotrimer association
H772A
site-directed mutagenesis, mutation of beta subunit Sip1 does not affect Sip1 function
H379A
-
site-directed mutagenesis, mutation of beta subunit Gal83 with little effect on Gal83 function
-
H380A
-
site-directed mutagenesis, mutation of beta subunit Sip2, mutation does not affect heterotrimer association
-
H384A
-
site-directed mutagenesis, mutation of beta subunit Gal83 causing a severe loss of function when assayed for growth on alternative carbon sources, the mutation does not affect heterotrimer association
-
H772A
-
site-directed mutagenesis, mutation of beta subunit Sip1 does not affect Sip1 function
-
E344K
-
mutation in the autoinhibitory domain, disruption of the hydrophilic interactions, yields a modest but marked increase in basal activity
L312D
-
mutation in the autoinhibitory domain, leads to marked enzymatic activation
L341D
-
mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain
L342D
-
mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain
L88A
-
mutation in the kinase domain, has decreased catalytic activity
M316E
-
mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain
R149E
-
mutation in the kinase domain, has decreased catalytic activity
R280A
-
mutation in the autoinhibitory domain, has no effect on kinase activity
additional information
K45R
-
site-directed mutagenesis, a dominant-negative mutant, expression leads to accumulation of lipids in cells
K45R
Q13131; Q9Y478; P54619
site-directed mutagenesis, a kinase dead mutant AMPK, the mutant is ineffective in inhibiting heterotetrameric K+-channel KCNQ1/KCNE1
R70Q
-
site-directed mutagenesis, marked increase in activity, largely AMP-independent
R70Q
Q13131; Q9Y478; P54619
site-directed mutagenesis, the constitutively active mutant is more effective in inhibiting heterotetrameric K+-channel KCNQ1/KCNE1 than the wild-type enzyme
T172D
-
site-directed mutagenesis, constitutively active mutant of AMPK, insensitive to metformin
T172D
site-directed mutagenesis of AMPK subunit alpha2, a phosphorylated-state mimic mutant. The activity of the T172D mutant kinase domain with and without AMPK kinase is about 40fold higher than that of the wild-type kinase domain treated with protein phosphatase 2A. The apo-form structure of the T172D mutant is essentially identical to that published for the wild type
R225Q
-
the mutation in gamma3 subunit leads to enhanced expression of Cd36 and cytochrome c in transgenic mice
R225Q
-
gain-of-function mutation, overexpression of the AMPK gamma3 subunit mutant increases mitochondrial biogenesis in glycolytic skeletal muscle, which is associated with an increase in expression of the co-activator PGC-1alpha and several transcription factors that regulate mitochondrial biogenesis, including NRF-1, NRF-2, and TFAM. Succinate dehydrogenase is also increased in transversal skeletal muscle sections of white gastrocnemius muscle, independent of changes in fiber type composition
D157A
-
AMPKalpha2 mutant, expression of a dominant-negative AMPK alpha results in a decreased ATP level and significantly compromised survival in hypoxia
additional information
-
aak-2 mutation and par-4 knockdown increase the sensitivity of worms to paraquat, and the double deficiency does not further increase sensitivity
additional information
-
a dominant negative AMP-activated protein kinase mutant abrogates rosiglitazone-stimulated Ser1177 phosphorylation and NO production in endothelial cells
additional information
-
activating mutations in AMPK can cause heart disease, detailed overview
additional information
-
AMPK silencing increases PDGF-induced proliferation of hepatic stellate cells
additional information
-
enzyme inhibition by expression of a dominant negative expression vector with kinase-dead form of AMPKalpha2
additional information
-
overexpression of the kinase-negative AMPK inhibits enzyme activation by 2-deoxyglucose
additional information
C-terminal truncation of AMPKalpha at residue 312 yields a protein that is active upon phosphorylation of Thr172 in the absence of beta and gamma subunits, which is refered to as the AMPK catalytic domain and commonly used to substitute for AMPK heterotrimeric complex in in vitro kinase assays
additional information
-
lipolysis is reduced in mutant with expression of a dominant-negative AMPK of in a null-mutant
additional information
-
AMPK subunit alpha2 and gamma3 knockoout mice show reduced inhibition of mTOR phosphorylation/activation and reduced mTOR signaling, overview
additional information
-
cells deficient in Tsc2, a tuberin encoded by gene tsc2, show cytoplasmic mislocalization of p27, which is reversible by inhibitors of the LKB1/AMPK pathway
additional information
-
construction of AMPK deficient ob/ob mice as a model for the metabolic syndrome, phenotype, overview. Activating mutations in AMPK can cause heart disease, detailed overview
additional information
-
construction of AMPKalpha1-KO mice, which show a splenomegaly possibly due to the massive amplification of erythroid nucleated cells, AMPKalpha1-KO mice are fully immunocompetent in vivo and display normal cell proliferation, humoral, cytotoxic and delayed-type hypersensitivity responses following antigen injection, phenotype, overview. AMPKalpha1-KO cells display increasing sensitivity to energetic stress in vitro, and are unable to maintain adequate ATP levels in response to ATP synthase inhibition, but the cells are able to respond to antigen stimulation in vitro, overview
additional information
-
construction of AMPKgamma3-knockout mice, which show impaired fasting-induced expression of skeletal musclelipid oxidative genes, while in mice overexpressing AMPKgamma3, an upregulation of lipid metabolic and mitochondrial gene expression occurs, overexpression or deletion of AMPKalpha2 subunit leads to abolishment of mitochondrial gene expression activation
additional information
-
LBK1-KO mice mutants show reduced phospho-AMPK content and AMPK activity, e.g. with substrate CREB, overview
additional information
-
lipolysis is reduced in mutant with expression of a dominant-negative AMPK of in a null-mutant
additional information
-
AMPK deficiency leads to ATP depletion in hepatocytes
additional information
-
construction of AMPK deficient fa/fa rats as a model for the metabolic syndrome, phenotype, overview. Activating mutations in AMPK can cause heart disease, detailed overview
additional information
-
defective AMPK signaling reduces the rate of substrate cycling between de novo lipogenesis and lipid oxidation, leading to suppressed thermogenesis, which accelerates body fat recovery and furthermore sensitizes skeletal muscle to dietary fat-induced impairments in PI3K/AMPK signaling, overview
additional information
-
downregulation of AMPK by microinjection of AMPK-RNAi in ventromedial hypothalamus results in suppressed glucagon and reduction of AMPKalpha-2 isozyme, but not of AMPKalpha-1 isozyme
additional information
-
overexpression of constitutively active AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis, downregulation of AMPK via adenoviral delivery of dominant-negative AMPK-alpha prevents CO2-induced Na,K-ATPase endocytosis
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
-
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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2 h, inactivation, MgATP2- in a low, not high salt buffer restores activity, not cAMP or in phosphate buffer
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.05 M Tris-HCl, pH 7.5, 0.05 M NaF, 0.005 M diphosphate, 1 mM EDTA, 1 mM EGTA and 1 mM DTT, 0.1 mM PMSF, soybean trypsin inhibitor, benzamidine, Brij-35, 50% w/v glycerol, stable for at least 2 months
-
-70°C, 0.5 mg protein/ml, frozen in liquid nitrogen, can be stored with no loss of activity
-
-80C, glycerol
-80°C, in 0.05 M Tris-HCl buffer, pH 7.4, 0.05 M NaF, 0.003 M EDTA, 0.002 M EGTA, 0.005 M DTT, 0.5 mM PMSF, 10% v/v glycerol, remains stable for at least 3 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
different recombinant His6-tagged subunit constructs from Escherichia coli strain BL21-CodonPlusTM (DE3)-RIPL by nickel affinity chromatography and dialysis
functional full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase from Escherichia coli strain CodonPlus(DE3)-RIPL by nickel affinity chromatography, dialysis and two steps of gel filtration
P54646; O43741; Q9UGI9
isozymes alpha1 and alpha2 from liver homogenates by subcellular fractionation and immunoprecipitation
-
kinase domain and catalytic kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
kinase domain and kinase domain/autoinhibitory fragments of AMPK alpha-subunit
-
partial
recombinant GST-tagged isozyme AMPK alpha1beta1gamma1 from Spodoptera frugiperda Sf21 cells by glutathione affinity and anion exchange chromatography, and gel filtration
-
recombinant GST-tagged isozyme AMPK beta1-alpha1 subunits fusion protein from COS-7 cells by glutathione affinity exchange chromatography
-
recombinant GST-tagged subunit beta1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, anion exchange chromatography, and ultrafiltration
recombinant His-tagged AMPK alpha2 mutant by affinity chromatography and gel filtration
recombinant His-tagged isozymes alpha1 and alpha2 from Escherichia coli by nickel affinity chromatography
-
recombinant untagged protein by automated multidimensional purification including adsorption chromatography and gel filtration, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenoviral expression of wild-type, dominant negative or constitutively active AMPK mutants. Transduction of INS832/13 cells
-
alpha, beta and subunit encoding genes, phylogenetic trees
AMPK alpha subunits (alpha1 and alpha2) tagged with green fluorescent protein at the N-terminus and co-expressed with beta and gamma subunits in CCL13 cells
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ATII cells infected with a hemagglutinin-tagged adenovirus carrying the dominant-negative mutant K45R of the AMPK alpha1 subunit or with an adenovirus expressing a constitutively active AMPK alpha variant or with an adenovirus expressing a constitutively active AMPK alpha variant in which Thr172 is replaced with aspartate in the truncated AMPK alpha subunit, comprising residues 1 to 312. A549 cells transfected with AMPK alpha1
-
cardiac-specific transgenic mice overexpressing a dominant-negative AMPKalpha2 subunit
-
cDNA identified with porcine cDNA
DNA and amino acid sequence determination and analysis, phylogenetic tree, real-time PCR expression analysis of the AMPK alpha, beta, and gamma subunits, overview
expression of a dominant negative kinase-dead form of AMPKalpha2 in HeLa cells
-
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
expression of alpha1 subunit alone or in combination with other subunits in Escherichia coli
expression of alpha2 subunit alone or in combination with other subunits in Escherichia coli
expression of beta1 subunit alone or in combination with other subunits in Escherichia coli
expression of beta2 subunit alone or in combination with other subunits in Escherichia coli
expression of gamma1 subunit alone or in combination with other subunits in Escherichia coli
expression of GST-fused constitutively active form of AMPK alpha1, residues 1-312, and of the kinase-dead mutant AMPK in HEK-193 cells
-
expression of GST-tagged wild-type AMPK beta1-alpha1 subunits fusion protein in COS-7 cells, and expression of beta1 residue 367 mutants in fusion to gamma1 subunit in COS-7 cells
-
expression of His6-tagged beta1(186-270)gamma1 complex and of GST-tagged isozyme AMPK alpha1beta1gamma1 in Spodoptera frugiperda Sf21 cells
-
expression of mutant enzymes in Escherichia coli and, via adenovirus transfection, in Hep-G2 cells
-
expression of short hairpin RNA for GFP-tagged AMPHalpha subunit in rat ventromedial hypothalamus via injection of the adeno-associated viral vector
-
expression of the AMPKalpha1 dominant negative mutant D175A in fibroblasts as GFP-tagged enzyme using an adenoviral transfection system
-
expression of wild-type and mutant AMPKalpha2 in human BJ fibroblast cells and in 786-0 renal carcinoma cells
-
functional His-tagged full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase is recombinantly expressed in Escherichia coli strain CodonPlus(DE3)-RIPL. All three subunits of AMPK alpha2beta2gamma3 are transcribed as a single tricistronic transcript driven by the T7 RNA polymerase promoter, allowing spontaneous formation of the heterotrimeric complex in the bacterial cytosol
P54646; O43741; Q9UGI9
gene PRKAA2, recombinant expression of kinase domain (residues 6-279) of the AMPK alpha2 mutant with an N-terminal His-tag and a tobacco etch virus (TEV) protease cleavage site via Escherichia coli cell-free system using the dialysis method
gene Prkab1, recombinant expression of GST-tagged subunit beta1 in Escherichia coli strain BL21(DE3)
gene Prkab2, recombinant expression of GST-tagged subunit beta2 in Escherichia coli strain BL21(DE3)
kinase domain and catalytic kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit. AMPK holoenzyme expressed in a tricistronic vector
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
recombinant coexpression of different His6-tagged subunit constructs in Escherichia coli strain BL21-CodonPlusTM (DE3)-RIPL, coexpression with biotin-ligase (BirA)
recombinant expression of C-terminally HA-tagged or N-terminally triple-FLAG-tagged isozyme in an enzyme-deficient Saccharomyces cerevisiae strain, expression of C-terminally GFP-tagged isozyme in haploid Saccharomyces cerevisiae
recombinant expression of His-tagged AMPK catalytic domain in Escherichia coli strain Rossetta (DE3)
transgenic mice overexpressing either the wild-type or the R225Q mutant subunit and knock-out mice
-
transgenic mouse constructed by injection of Rattus norvegicus alpha2 subunit cDNA
-
transient expression of wild-type and mutant enzymes in COS-7 cells, co-expression with histone deacetylase 5
-
wild-type HA-tagged AMPKalpha1, FLAG-tagged AMPKbeta1, HA-tagged AMPKgamma1, constitutively active HA-tagged AMPKgamma1 mutant R70Q , kinase dead mutant HA-tagged AMPKalpha1 mutant K45R, and wild type HA-tagged AMPK alpha2, recombinant expression in Xenopus laevis oocytes. Coexpression with human KCNQ1/KCNE1. AMPK inhibites voltage-gated outward currents in KCNQ1/KCNE1-expressing Xenopus oocytes. Coexpression of the AMP-activated protein kinase, i.e. AMPKalpha1, AMPKbeta1, and AMPKgamma1
Q13131; Q9Y478; P54619
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
-
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
-
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3 days of recurrent insulin-induced hypoglycaemia results in an increase in the gene expression of alpha1- and alpha2AMPK in the whole hypothalamus and in the dorso-mediobasal hypothalamus
-
alpha1 and alpha2 AMPK siRNAs selectively suppress AMPKalpha1 and AMPKalpha2 protein, respectively. AMPKalpha1 and AMPKalpha2 proteins are reduced to 6 and 1% of respective controls. Combined treatment with both alpha1 and alpha2 AMPK siRNAs lead to 66 and 92% reduction of AMPKalpha1 and AMPKalpha2 protein, respectively
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AMPKalpha mRNA levels increase continuously throughout exposure to 26°C, reaching 5.6times more after 6 h at 26°C than in the 12°C controls
AMPKalpha1 repression causes a 37% compensational increase in AMPKalpha2 protein
-
enzyme activity significantly increases during ischemia, remaining activated during reperfusion
-
in the muscle subunit AMPK-gamma mRNA is significantly up-regulated at low salinity relative to controls. Muscle and hepatopancreas show increases in enzyme protein after 6 h exposure to low salinity, but there are no differences seen after long term acclimation
loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
overexpression of AMPK dominant negative mutant abolishes statin-induced reduction of O2- in BAEC
-
relative expression of alpha, beta, and gamma isoforms of AMPK is greatest in muscle and MAC-T cells
-
siRNA knockdown of AMPK, which ameliorates the IFNgamma-induced increase in epithelial permeability and decrease in transepithelial electrical resistance
-
the expression of enzyme isoform AMPKalpha2 significantly increases in the hepatopancreas of fish exposed to 1 week of overwinter starvation conditions. The expression of isoform AMPKalpha2 significantly increases in the adipose tissue of fish exposed to 4 week of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKbeta1b significantly increases in the hepatopancreas of fish exposed to 8 weeks of overwinter starvation conditions. The expression of isoform AMPKbeta1b significantly increases in the adipose tissue of fish exposed to 1 week of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKbeta2 significantly increases in the hepatopancreas of fish exposed to 12 weeks of overwinter starvation conditions. The expression of isoform AMPKbeta2 significantly increases in the adipose tissue of fish exposed to 8 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma1 significantly increases in the hepatopancreas of fish exposed to 12 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma1 significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma2a significantly increases in the hepatopancreas of fish exposed to 16 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma2a significantly increases in the adipose tissue of fish exposed to 8 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma2b significantly increases in the hepatopancreas of fish exposed to 8 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma2b significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma3 significantly increases in the hepatopancreas of fish exposed to 16 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma3 significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of isoform AMPKalpha1 significantly increases in the hepatopancreas of fish exposed to 1 week of overwinter starvation conditions. The expression enzyme isoform AMPK alpha1 significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of various enzyme isoform AMPKbeta1a significantly increases in the hepatopancreas of fish exposed to 16 weeks of overwinter starvation conditions. The expression of isoform AMPKbeta1a significantly increases in the adipose tissue of fish exposed to 1 week of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the mRNA level of subunit AMPK-alpha is up-regulated in the hepatopancreas and muscle after acute low-salinity stress at 3 psu for 6 h compared with control salinity at 20 psu. After 8-week salinity stress at 3 psu, AMPK-alpha and mRNA level in the hepatopancreas is significantly higher than those of the control at 30 psu. Muscle and hepatopancreas show increases in enzyme protein after 6 h exposure to low salinity, but there are no differences seen after long term acclimation
the mRNA level of subunit AMPK-beta is up-regulated in the hepatopancreas and muscle after acute low-salinity stress at 3 psu for 6 h compared with control salinity at 20 psu. After 8-week salinity stress at 3 psu, AMPK-beta mRNA level in the hepatopancreas is significantly higher than those of the control at 30 psu. Muscle and hepatopancreas show increases in enzyme protein after 6 h exposure to low salinity, but there are no differences seen after long term acclimation
loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
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loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
industry
-
AMPK as a molecular target capable of modifying energy substrate utilization may result in the development of new technologies that increase milk production or modify milk composition during periods of increased energy demand
medicine
pharmacology
-
selective AMPK activators are potential therapeutics in type 2 diabetes
additional information
drug development
-
pharmacological activators of AMPK can act as treatments for diabetes and the metabolic syndrome
drug development
-
activating AMPK may have therapeutic potential in treating dry macular degeneration
drug development
-
AMPK is a highly attractive target for the prevention and treatment of type 2 diabetes and other disorders of the metabolic syndrome, and to curb the prevalence and costs of type 2 diabetes
drug development
-
AMPK is a highly attractive target for the prevention and treatment of type 2 diabetes and other disorders of the metabolic syndrome, and to curb the prevalence and costs of type 2 diabetes
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK represents an attractive therapeutic target for vascular disease treatment
drug development
-
AMPK represents an attractive therapeutic target for vascular disease treatment
drug development
-
AMPK represents an attractive therapeutic target for vascular disease treatment
drug development
-
targeting SIRT1-AMPK pathway may serve as a new target for the development of new anti HIV-1 agents
drug development
-
the AMPK inhibitor 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine may serve as a useful molecule in both basic and clinical research on adipogenesis and as a potential lead compound for the treatment of obesity
drug development
-
the glucose-sensitive stimulatory impact of BLX-1002 on beta-cell function associated with AMPK activation may translate into substantial clinical benefits of the drug in the management of type 2 diabetes, by avoidance of hypoglycemia
drug development
-
triterpenoids are potential hypoglycemic components of the plant and the mechanism underlying their action involves AMPK
drug development
AMP-activated protein kinase (AMPK) is a potential target for drug design against metabolic syndrome, obesity and type 2 diabetes
drug development
P54646; O43741; Q9UGI9
AMPK alpha2beta2gamma3 is an attractive target for drug development for diabetes and metabolic syndrome
drug development
design and development of isoform-selective AMPK activators that are likely to be useful for the treatment of cardiovascular and metabolic diseases
medicine
-
compounds that would cause activation of enzyme in skeletal muscle promise to be attractive agents for therapeutic intervention
medicine
-
decreasing the ischaemic-induced activation of AMPK may be a therapeutic approach to treating ischaemic heart disease, AMPK may be an important pharmacological target for improving cardiac efficiency following ischaemia
medicine
-
defects or disuse of the AMPK signaling system would be predicted to result in many of the metabolic perturbations observed in type 2 diabetes mellitus
medicine
-
implication of AMPK in the pathogenesis of chronic intestinal inflammatory conditions, such as inflammatory bowel disease
medicine
-
enzyme inhibition is a viable therapeutic strategy to prevent ischemic brain injury following stroke
medicine
-
the enzyme can be an alternative therapeutic approach to preventing and managing obesity
additional information
AMPK is an earlier indicator of temperature stress in rock crabs than HSP70, especially during the initial response to high temperatures. AMPK activity is a cellular marker that indicates a thermal threshold, called the pejus temperature
additional information
AMPK is an earlier indicator of temperature stress in rock crabs than HSP70, especially during the initial response to high temperatures. AMPK activity is a cellular marker that indicates a thermal threshold, called the pejus temperature
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EXTERNAL LINKS (specific for EC-Number 2.7.11.31)
Transporter Classification Database (TCDB): 8.A.104.1.1
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Release 2023.1 (January 2023)
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