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Information on EC 2.7.11.31 - [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase and Organism(s) Mus musculus
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2.7.11.31 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinaseIUBMB Comments
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) . Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase . GTP can act instead of ATP
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Word Map
- 2.7.11.31
- 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
-
metformin-induced
- phenformin
-
energy-sensing
-
insulin-independent
- medicine
- industry
- pharmacology
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, 
more
topSYNONYM 
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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AMP-activated protein kinase
AMPK
beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
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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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[hydroxymethylglutaryl-CoA reductase (NADPH2)] 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
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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]
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 + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + bis(5'-nucleosyl)-tetraphosphatase
ADP + [bis(5'-nucleosyl)-tetraphosphatase]phosphate
-
-
-
-
?
ATP + collapsing response mediator protein-2
ADP + [collapsing response mediator protein-2]phosphate
-
-
-
-
?
ATP + dihydropyrimidinase-like 2
ADP + [dihydropyrimidinase-like 2]phosphate
-
-
-
-
?
ATP + dynein intermediate chain 2
ADP + [dynein intermediate chain 2]phosphate
-
-
-
-
?
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 + glyceraldehyde-3-phosphate dehydrogenase
ADP + [glyceraldehyde-3-phosphate dehydrogenase]phosphate
-
-
-
-
?
ATP + heterogeneous nuclear ribonucleoproteins A2/B1
ADP + [heterogeneous nuclear ribonucleoproteins A2/B1]phosphate
-
-
-
-
?
ATP + JAK1
ADP + phosphorylated JAK1
-
phosphorylation at Ser515 and Ser518
-
-
?
ATP + neurofilament triplet L protein
ADP + [neurofilament triplet L protein]phosphate
-
-
-
-
?
ATP + Ngg1 interacting factor 3-like 1
ADP + [Ngg1 interacting factor 3-like 1]phosphate
-
-
-
-
?
ATP + NmrA-like family domain containing 1
ADP + [NmrA-like family domain containing 1]phosphate
-
-
-
-
?
ATP + 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 + telomerase-binding protein p23
ADP + [telomerase-binding protein p23]phosphate
-
-
-
-
?
ATP + tripeptidyl-peptidase 2
ADP + [tripeptidyl-peptidase 2]phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase 2]
ADP + [acetyl-CoA carboxylase 2] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
-
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
ATP + ATF1
ADP + phospho-ATF1
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
phosphorylation at Ser63 and Ser267, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + ATF2
ADP + phospho-ATF2
-
recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + 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
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phosphorylation at Ser119, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREBL2
ADP + phospho-CREBL2
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recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREM
ADP + phospho-CREM
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREM
ADP + phospho-CREM
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phosphorylation at Ser71 and Ser192, recombinant AMPK composed by subunits alpha2beta2gamma2
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-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
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-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
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HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
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-
?
ATP + p27
ADP + phospho-p27
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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
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-
?
ATP + p27
ADP + phospho-p27
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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
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-
?
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
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activation
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-
?
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
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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
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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
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phosphorylation in the CaM-binding domain at Ser815, substrate from chicken, determination of the phosphorylation site by mass spectrometric analysis
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-
?
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
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-
?
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
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-
?
additional information
?
-
-
AMP-activated protein kinase phosphorylates transcription factors of the CREB family
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 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 + 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 + 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 + [acetyl-CoA carboxylase 2]
ADP + [acetyl-CoA carboxylase 2] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] 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
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z)-2-[(3-hydroxyphenyl)amino]-5-(1H-indol-3-ylmethylidene)-1,3-thiazol-4(5H)-one
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A134974
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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
C75
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rapidly reduces the level of the phosphorylated AMPKalpha subunit in the hypothalamus. Also reduces pAMPK levels in fasted mice that have elevated hypothalamic pAMPK
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
N-(2-[[2-(1H-indol-3-yl)ethyl]amino]-2-oxoethyl)-3-phenyl-2,1-benzoxazole-5-carboxamide
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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
-
inhibits AMPK in a dose dependent manner. Suppresses AMPK activity during the early phase of adipogenic differentiation, which indicates that suppressed activation of AMPK may inhibit the mitotic clonal expansion process of preadipocytes. Levels of phosphorylated AMPKalpha and total AMPKalpha are not affected by 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, inhibits AMPK, whereby restores acid secretion
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+)-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
(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
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
adiponectin
-
activation of AMPK, which is mediated via cell surface receptor AdipoR1
-
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
-
Calmodulin
-
AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
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
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
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
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 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-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
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
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
resveratrol
-
increases the phosphorylation status of AMPK in wild-type MEFs. Effect of resveratrol on AMPK is mediated via LKB1
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
selective expression of the AMPKalpha1 catalytic subunit in lymphoid cells
additional information
-
AMPK is widely expressed throughout the brain, including several areas controlling food intake and neuroendocrine function
-
gastrocnemius, tibialis anterior, heart, and epitrochlearis muscle
additional information
-
present in BMM cells. Osteoclasts and macrophages lack AMPK beta2 subunit expression
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
-
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
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
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
physiological function
-
activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease
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 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 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
-
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
-
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 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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AAPK1_MOUSE
559
0
63929
Swiss-Prot
other Location (Reliability: 4)
AAPK2_MOUSE
552
0
62022
Swiss-Prot
other Location (Reliability: 1)
Q3TUQ7_MOUSE
550
0
62728
TrEMBL
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
trimer
additional information
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
additional information
-
the alpha1-subunit isoform accounts for 90% of the total AMPK in vascular smooth muscle
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R225Q
additional information
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cardiac-specific transgenic mice overexpressing a dominant-negative AMPKalpha2 subunit
-
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
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
-
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
medicine
-
compounds that would cause activation of enzyme in skeletal muscle promise to be attractive agents for therapeutic intervention
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fryer, L.G.; Foufelle, F.; Barnes, K.; Baldwin, S.A.; Woods, A.; Carling, D.
Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells
Biochem. J.
363
167-174
2002
Mus musculus
Xing, Y.; Musi, N.; Fujii, N.; Zou, L.; Luptak, I.; Hirshman, M.F.; Goodyear, L.J.; Tian, R.
Glucose metabolism and energy homeostasis in mouse hearts overexpressing dominant negative alpha2 subunit of AMP-activated protein kinase
J. Biol. Chem.
278
28372-28377
2003
Mus musculus
Daval, M.; Diot-Dupuy F.; Bazin, R.; Hainault, I.; Viollet, B.; Vaulont, S.; Hajduch, E.; Ferr, P.; Foufelle, F.
Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes
J. Biol. Chem.
280
25250-25257
2005
Mus musculus, Rattus norvegicus
Horman, S.; Morel, N.; Vertommen, D.; Hussain, N.; Neumann, D.; Beauloye, C.; El Najjar, N.; Forcet, C.; Viollet, B.; Walsh, M.P.; Hue, L.; Rider, M.H.
AMP-activated protein kinase phosphorylates and desensitizes smooth muscle myosin light chain kinase
J. Biol. Chem.
283
18505-18512
2008
Mus musculus
Long, Y.C.; Zierath, J.R.
Influence of AMP-activated protein kinase and calcineurin on metabolic networks in skeletal muscle
Am. J. Physiol. Endocrinol. Metab.
295
E545-E552
2008
Mus musculus
Short, J.D.; Houston, K.D.; Dere, R.; Cai, S.L.; Kim, J.; Johnson, C.L.; Broaddus, R.R.; Shen, J.; Miyamoto, S.; Tamanoi, F.; Kwiatkowski, D.; Mills, G.B.; Walker, C.L.
AMP-activated protein kinase signaling results in cytoplasmic sequestration of p27
Cancer Res.
68
6496-6506
2008
Mus musculus
Mayer, A.; Denanglaire, S.; Viollet, B.; Leo, O.; Andris, F.
AMP-activated protein kinase regulates lymphocyte responses to metabolic stress but is largely dispensable for immune cell development and function
Eur. J. Immunol.
38
948-956
2008
Mus musculus
Hardie, D.G.
Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease
FEBS Lett.
582
81-89
2008
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Dictyostelium discoideum, Drosophila melanogaster, Giardia intestinalis, Homo sapiens, Mus musculus, Physcomitrium patens, Rattus norvegicus, Schizosaccharomyces pombe, Trypanosoma brucei
Thomson, D.M.; Herway, S.T.; Fillmore, N.; Kim, H.; Brown, J.D.; Barrow, J.R.; Winder, W.W.
AMP-activated protein kinase phosphorylates transcription factors of the CREB family
J. Appl. Physiol.
104
429-438
2008
Mus musculus
Cheung, W.D.; Hart, G.W.
AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation
J. Biol. Chem.
283
13009-13020
2008
Mus musculus
eshmukh, A.S.; Treebak, J.T.; Long, Y.C.; Viollet, B.; Wojtaszewski, J.F.; Zierath, J.R.
Role of adenosine 5'-monophosphate-activated protein kinase subunits in skeletal muscle mammalian target of rapamycin signaling
Mol. Endocrinol.
22
1105-1112
2008
Mus musculus
Hegarty, B.D.; Turner, N.; Cooney, G.J.; Kraegen, E.W.
Insulin resistance and fuel homeostasis: the role of AMP-activated protein kinase
Acta Physiol. (Oxf.)
196
129-145
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Oakhill, J.S.; Scott, J.W.; Kemp, B.E.
Structure and function of AMP-activated protein kinase
Acta Physiol. (Oxf.)
196
3-14
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe, Sus scrofa
McBride, A.; Hardie, D.G.
AMP-activated protein kinase--a sensor of glycogen as well as AMP and ATP?
Acta Physiol. (Oxf.)
196
99-113
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Zhang, F.; Dey, D.; Braenstroem, R.; Forsberg, L.; Lu, M.; Zhang, Q.; Sjoeholm, A.
BLX-1002, a novel thiazolidinedione with no PPAR affinity, stimulates AMP-activated protein kinase activity, raises cytosolic Ca2+, and enhances glucose-stimulated insulin secretion in a PI3K-dependent manner
Am. J. Physiol. Cell Physiol.
296
C346-C354
2009
Mus musculus
Choi, J.S.; Park, C.; Jeong, J.W.
AMP-activated protein kinase is activated in Parkinsons disease models mediated by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
Biochem. Biophys. Res. Commun.
391
147-151
2010
Homo sapiens, Mus musculus
Gao, Y.; Zhou, Y.; Xu, A.; Wu, D.
Effects of an AMP-activated protein kinase inhibitor, compound C, on adipogenic differentiation of 3T3-L1 cells
Biol. Pharm. Bull.
31
1716-1722
2008
Mus musculus
Gundewar, S.; Calvert, J.W.; Jha, S.; Toedt-Pingel, I.; Ji, S.Y.; Nunez, D.; Ramachandran, A.; Anaya-Cisneros, M.; Tian, R.; Lefer, D.J.
Activation of AMP-activated protein kinase by metformin improves left ventricular function and survival in heart failure
Circ. Res.
104
403-411
2009
Mus musculus, Mus musculus C57/BL6J
Zou, M.H.; Wu, Y.
AMP-activated protein kinase activation as a strategy for protecting vascular endothelial function
Clin. Exp. Pharmacol. Physiol.
35
535-545
2008
Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces sp.
Li, C.; Keaney, J.F.
AMP-activated protein kinase: a stress-responsive kinase with implications for cardiovascular disease
Curr. Opin. Pharmacol.
10
111-115
2010
Saccharomyces cerevisiae, Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Beck Jorgensen, S.; ONeill, H.M.; Hewitt, K.; Kemp, B.E.; Steinberg, G.R.
Reduced AMP-activated protein kinase activity in mouse skeletal muscle does not exacerbate the development of insulin resistance with obesity
Diabetologia
52
2395-2404
2009
Mus musculus
Foeller, M.; Sopjani, M.; Koka, S.; Gu, S.; Mahmud, H.; Wang, K.; Floride, E.; Schleicher, E.; Schulz, E.; Muenzel, T.; Lang, F.
Regulation of erythrocyte survival by AMP-activated protein kinase
FASEB J.
23
1072-1080
2009
Homo sapiens, Mus musculus
Setsuie, R.; Suzuki, M.; Kabuta, T.; Fujita, H.; Miura, S.; Ichihara, N.; Yamada, D.; Wang, Y.L.; Ezaki, O.; Suzuki, Y.; Wada, K.
Ubiquitin C-terminal hydrolase-L3-knockout mice are resistant to diet-induced obesity and show increased activation of AMP-activated protein kinase in skeletal muscle
FASEB J.
23
4148-4157
2009
Mus musculus
Quinn, J.M.; Tam, S.; Sims, N.A.; Saleh, H.; McGregor, N.E.; Poulton, I.J.; Scott, J.W.; Gillespie, M.T.; Kemp, B.E.; van Denderen, B.J.
Germline deletion of AMP-activated protein kinase beta subunits reduces bone mass without altering osteoclast differentiation or function
FASEB J.
24
275-285
2010
Mus musculus, Mus musculus C57/BL6J
Cheng, H.L.; Huang, H.K.; Chang, C.I.; Tsai, C.P.; Chou, C.H.
A cell-based screening identifies compounds from the stem of Momordica charantia that overcome insulin resistance and activate AMP-activated protein kinase
J. Agric. Food Chem.
56
6835-6843
2008
Mus musculus
Choi, H.C.; Song, P.; Xie, Z.; Wu, Y.; Xu, J.; Zhang, M.; Dong, Y.; Wang, S.; Lau, K.; Zou, M.H.
Reactive nitrogen species is required for the activation of the AMP-activated protein kinase by statin in vivo
J. Biol. Chem.
283
20186-20197
2008
Bos taurus, Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Chan, A.Y.; Dolinsky, V.W.; Soltys, C.L.; Viollet, B.; Baksh, S.; Light, P.E.; Dyck, J.R.
Resveratrol inhibits cardiac hypertrophy via AMP-activated protein kinase and Akt
J. Biol. Chem.
283
24194-24201
2008
Mus musculus, Rattus norvegicus
Garcia-Roves, P.M.; Osler, M.E.; Holmstroem, M.H.; Zierath, J.R.
Gain-of-function R225Q mutation in AMP-activated protein kinase gamma3 subunit increases mitochondrial biogenesis in glycolytic skeletal muscle
J. Biol. Chem.
283
35724-35734
2008
Mus musculus
Kola, B.
Role of AMP-activated protein kinase in the control of appetite
J. Neuroendocrinol.
20
942-951
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Spasic, M.R.; Callaerts, P.; Norga, K.K.
AMP-activated protein kinase (AMPK) molecular crossroad for metabolic control and survival of neurons
Neuroscientist
15
309-316
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
Sidani, S.; Kopic, S.; Socrates, T.; Kirchhoff, P.; Foeller, M.; Murek, M.; Capasso, A.; Geibel, J.P.
AMP-activated protein kinase: a physiological off switch for murine gastric acid secretion
Pflugers Arch.
459
39-46
2009
Mus musculus
Wang, Y.; Viollet, B.; Terkeltaub, R.; Liu-Bryan, R.
AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages
Ann. Rheum. Dis.
75
286-294
2016
Mus musculus (Q5EG47), Mus musculus C57BL/6/129 (Q5EG47)
Eom, J.W.; Kim, T.Y.; Seo, B.R.; Park, H.; Koh, J.Y.; Kim, Y.H.
Identifying new AMP-activated protein kinase inhibitors that protect against ischemic brain injury
ACS Chem. Neurosci.
10
2345-2354
2019
Mus musculus
EXTERNAL LINKS (specific for EC-Number 2.7.11.31)
Transporter Classification Database (TCDB): 8.A.104.1.1
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