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Information on EC 2.7.11.31 - [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase and Organism(s) Rattus norvegicus and UniProt Accession P54645

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IUBMB 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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Rattus norvegicus
UNIPROT: P54645
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AMP-activated protein kinase
-
3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
-
-
-
-
3-hydroxy-3-methylglutaryl-CoA reductase kinase
-
-
-
-
adenosine monophosphateactivated protein kinase
-
-
AMP-activated protein kinase
AMP-activated protein kinase alpha
-
-
AMPKalpha
-
isoform
AMPKalpha1beta1gamma1
-
isoform
beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
-
-
-
-
hydroxymethylglutaryl coenzyme A reductase kinase
-
-
-
-
hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating)
-
-
-
-
reductase kinase
-
-
-
-
[hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase
-
-
-
-
additional information
-
AMPK is a member of the serine/threonin protein kinases, as well as of a metabolite-sensing kinase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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 hide
172522-01-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
show the reaction diagram
i.e. SAMS peptide
-
-
?
ATP + 3-hydroxy-3-methyl-glutaryl-CoA reductase
ADP + [3-hydroxy-3-methyl-glutaryl-CoA reductase]phosphate
show the reaction diagram
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
show the reaction diagram
-
phosphorylation at Ser79
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
show the reaction diagram
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
show the reaction diagram
-
-
-
-
?
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
show the reaction diagram
-
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + [adipose hormone-sensitive lipase] phosphate
show the reaction diagram
-
-
-
-
?
ATP + bovine serum albumin
ADP + [bovine serum albumin] phosphate
show the reaction diagram
-
fraction V
-
-
?
ATP + casein
ADP + casein phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 8%, high MW-kinase 48%
-
-
?
ATP + dephospho-alpha,beta-tubulin
ADP + [alpha,beta-tubulin] phosphate
show the reaction diagram
-
relative kinase activity high MW-kinase 15%
-
-
?
ATP + dephospho-beta-tubulin
ADP + [beta-tubulin]phosphate
show the reaction diagram
-
-
-
-
?
ATP + glycerophosphate acyltransferase
ADP + [glycerophosphate acyltransferase]phosphate
show the reaction diagram
-
-
-
-
?
ATP + glycogen synthase
ADP + [glycogen synthase] phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 7%, high MW-kinase 87%
-
-
?
ATP + heavy meromyosin
ADP + [heavy meromyosin] phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 100%
-
-
?
ATP + histone 2A
?
show the reaction diagram
-
-
-
-
?
ATP + histone H1
ADP + phosphohistone H1
show the reaction diagram
-
-
-
-
?
ATP + histone H1 (IIIS)
ADP + [histone H1 (IIIS)] phosphate
show the reaction diagram
-
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
show the reaction diagram
-
relative kinase activity for low-MW kinase 38%, high MW-kinase 159%
-
-
?
ATP + histone VIIIS
ADP + [histone VIIIS] phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 65%, high MW-kinase 141%
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
show the reaction diagram
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
show the reaction diagram
ATP + MAP-2
ADP + MAP-2 phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 14%, high MW-kinase 566%
-
-
?
ATP + myelin basic protein
ADP + [myelin basic protein] phosphate
show the reaction diagram
-
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
show the reaction diagram
-
relative kinase activity for low-MW kinase 4%, high MW-kinase 27%
-
-
?
ATP + peptide SAMS
ADP + phosphorylated peptide SAMS
show the reaction diagram
-
-
-
-
?
ATP + phosphorylase B
ADP + [phosphorylase B] phosphate
show the reaction diagram
-
relative kinase activity high MW-kinase 12%
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 2%
-
-
?
ATP + protamine
ADP + protamine phosphate
show the reaction diagram
-
relative kinase activity for low-MW kinase 24%, high MW-kinase 38%
-
-
?
ATP + protein GFAP
ADP + [protein GFAP]phosphate
show the reaction diagram
-
-
-
-
?
ATP + protein NF-L
ADP + [protein NF-L]phosphate
show the reaction diagram
-
-
-
-
?
ATP + rabbit muscle glycogen synthase
ADP + [rabbit muscle glycogen synthase] phosphate
show the reaction diagram
-
rabbit muscle glycogen synthase
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
show the reaction diagram
-
-
-
-
?
ATP + synapsin 1
ADP + [synapsin 1] phosphate
show the reaction diagram
-
as good substrate as hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 151%, high MW-kinase 103%
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
show the reaction diagram
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
show the reaction diagram
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
ATP + [malonylCoAdecarboxylase]
ADP + [malonylCoAdecarboxylase]phosphate
show the reaction diagram
-
-
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
show the reaction diagram
ATP + [peptide QKFQRELSTKWVLN]
ADP + [peptide QKFQRELSTKWVLN] phosphate
show the reaction diagram
-
a peptide derived from glucose hexokinase regulatory protein, residues 474-487
-
-
?
ATP + [peptide SAMS]
ADP + [peptide SAMS] phosphate
show the reaction diagram
-
-
-
-
?
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
show the reaction diagram
-
-
-
-
?
CTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
CDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
-
-
-
-
?
dATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
dADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
-
phosphorylation at about 90% the rate of ATP
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
show the reaction diagram
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
show the reaction diagram
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
show the reaction diagram
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
show the reaction diagram
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
show the reaction diagram
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-dAMP
-
activation, can replace AMP or ADP
Calmodulin
-
requirement, Ca2+/calmodulin dependent kinase, no phosphorylation of substrate observed in absence
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2'-deoxy-ATP
-
-
2'5'-dideoxyadenosine
-
inhibits ability of interleukin-6 to activate AMPK
5'-fluorosulfonylbenzoyladenosine
-
-
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C
8-bromo-AMP
-
-
A-769662
-
allosterically regulates AMPK activity
adenine-9-beta-D-arabinofuranoside
-
-
adenosine
-
-
adenosine-5'-tetraphospho-5'-adenosine
-
i.e. AP4A, inhibits in the presence of AMP
compound C
Cu2+
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, 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
-
glycerol
-
25% v/v, reversible inhibition
hydroxymethylglutaryl-CoA
-
only with hydroxymethylglutaryl-CoA reductase as substrate
Inhibitor W-7
-
specific Ca2+/calmodulin-dependent kinase inhibitor
iodotubercidin
-
-
leptin
-
has a tissue-specific effect on AMPK, in the hypothalamus, it decreases hypothalamic AMPK activity
-
metformin
-
can inhibit the stimulatory effect of dexamethasone in primary hypothalamic culture, blocks the AMPK phosphorylation induced by low glucose in primary cultures of hypothalamic neurones
naringin
-
inhibits enzyme phosphorylation
propranolol
-
effects of interleukin-6 on both AMPK activity and energy state are inhibited by coincubation with propranolol, suggesting involvement of beta-adrenergic signaling
propylthiouracil
-
inhibits stimulation by thyroid hormones
protein phosphatase C
-
-
-
sucrose
-
sucrose-drinking animals have lower hypothalamic AMPK activity compared to saline-drinking control rats
Trifluperazine
-
specific Ca2+/calmodulin-dependent kinase inhibitor
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',3',5'-tri-O-acetyl-N-(3-hydroxyphenyl)adenosine
-
EC50 of 0.3273 mM
-
5'-AMP
5-amino-4-imidazolecarboxamide ribonucleoside
-
-
-
5-amino-4-imidazolecarboxamide ribotide
-
-
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
5-aminoimidazole-4-carboxamide riboside
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, activates the phosphorylation of peptide QKFQRELSTKWVLN 4fold, kinetics, overview
A-769662
adenosine
-
-
adiponectin
-
-
-
alpha,beta-methylene-ADP
-
allosteric activator, can replace ADP, with 66% efficiency with bovine serum albumin as substrate
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
-
activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
calyculin A
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
CaMKKbeta
-
phosphorylates
-
cantharidin
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
CDP
-
allosteric activator
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
D-glucose
-
-
D-ribose 5-phosphate
-
-
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
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
-
Insulin
-
insulin-induced hypoglycaemia in rats increases AMPK phosphorylation and alpha2AMPK activity in the arcuate nucleus/dorso-mediobasal hypothalamus and paraventricular nucleus
-
interleukin-1
-
induces nitric oxide-dependent activation of AMPK
-
interleukin-6
isoproterenol
-
-
leptin
-
metformin
microcystin-LR
-
stimulation of activating AMPK phosphorylation at Thr172
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
okadaic acid
-
stimulation of activating AMPK phosphorylation at Thr172, activation is antagonized by naringin
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
-
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
rotenone
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
tautomycin
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
thiazolidinediones
-
-
UDP
-
allosteric activator
[([5-(5-oxo-4,5-dihydro-1,2-oxazol-3-yl)furan-2-yl]phosphoryl)bis(oxy)methylene]bis(2-methylpropanoate)
-
i.e. C13
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.315
ATP
0.0029
histone H1
-
pH 6.5, 30°C, low-MW kinase
-
0.00085
hydroxymethylglutaryl-CoA reductase
-
pH 6.5, 30°C, low-MW kinase
0.055
peptide SAMS
-
-
0.101
peptide QKFQRELSTKWVLN
-
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
purified recombinant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
low-MW kinase
7.5
-
assay at
additional information
-
pI: 5.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7
-
about half-maximal activity at pH 5.5 and 7.0, low-MW kinase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha1 subunit
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
intrapulmonary smooth muscle
Manually annotated by BRENDA team
-
primary hypothalamic or adipose cells
Manually annotated by BRENDA team
-
alveolar epithelial type II cell, ATII cell
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
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
-
Manually annotated by BRENDA team
additional information
-
differential localization patterns of AMPKalpha 1 and AMPKalpha2
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AAPK1_RAT
559
0
63973
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105000
-
2 * 105000, SDS-PAGE
110000 - 125000
-
low-MW kinase, gel filtration
180000
-
x * 180000, SDS-PAGE
205000
-
gel filtration
30000
-
beta-subunit, predicted protein sequence
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
380000
-
rat, gel filtration
40000
-
1 * 63000 + 1 * 40000 + ?, alpha and beta subunit, SDS-PAGE
56000
-
x * 56000, SDS-PAGE
560000 - 600000
-
high-MW kinase, gel filtration
58000
-
x * 58000, SDS-PAGE
63000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
heterotrimer, complex structure determination and analysis by mass spectrometry, dynamic light and small-angle X-ray scattering and transmission electrom microscopy, modeling, overview
dimer
-
2 * 105000, SDS-PAGE
heterotrimer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
S485A
-
site-directed mutagenesis, non-phosphorylatable mutant
S485D
-
site-directed mutagenesis
T172A
-
site-directed mutagenesis
T172D
-
site-directed mutagenesis
T172E
-
site-directed mutagenesis
T258A
-
site-directed mutagenesis, non-phosphorylatable mutant
T258D
-
site-directed mutagenesis
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
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
2 h, inactivation, MgATP2- in a low, not high salt buffer restores activity, not cAMP or in phosphate buffer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
about 10% decrease of activity after each freeze-thawing
-
highly labile enzyme
-
protease inhibitors stabilizes enzyme
-
very stable at either 4°C or -20°C when in microsomes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-196°C, stored in liquid nitrogen, stable for several months
-
-20°C, can be stored in buffer containing 50% glycerol for up to a month
-
-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
-
-80°C, 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
-
-80°C, partially purified preparation, stable to freezing
-
4°C, unstable when solubilized, loses 90% activity within 3 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant untagged protein by automated multidimensional purification including adsorption chromatography and gel filtration, overview
catalytic subunit alpha
-
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
-
low-MW kinase
-
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 untagged protein by automated multidimensional purification including adsorption chromatography and gel filtration, overview
wild-type and mutant enzymes, expressed in bacteria
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of alpha1 subunit alone or in combination with other subunits in Escherichia coli
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
-
cDNA identified with porcine cDNA
-
expressed in HEK-293 cells
-
expressed in Sf9 insect cells and Escherichia coli strain BL21 (DE3)
-
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
-
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-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 short hairpin RNA for GFP-tagged AMPHalpha subunit in rat ventromedial hypothalamus via injection of the adeno-associated viral vector
-
expression of wild-type and mutant AMPKalpha2 in human BJ fibroblast cells and in 786-0 renal carcinoma cells
-
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
-
overexpression of HA-tagged AMPK in ATII cells
-
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
-
sequence analysis of cDNA clones encoding the subunits
-
transfection of CCL13 cells
-
transfections of COS7 cells
-
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
-
enzyme activity significantly increases during ischemia, remaining activated during reperfusion
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
pharmacology
-
selective AMPK activators are potential therapeutics in type 2 diabetes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ingebritsen, T.S.; Parker, R.A.; Gibson, D.M.
Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system
J. Biol. Chem.
256
1138-1144
1981
Rattus norvegicus
Manually annotated by BRENDA team
Carling, D.; Clarke, P.R.; Hardie, D.G.
Adenosine monophosphate-activated protein kinase: hydroxymethylglutaryl-CoA reductase kinase
Methods Enzymol.
200
362-371
1991
Rattus norvegicus, Rattus norvegicus Wistar
Manually annotated by BRENDA team
Stapleton, D.; Mitchelhill, K.I.; Gao, G.; Widmer, J.; Michell, B.J.; Teh, T.; House, C.M.; Fernandez, C.S.; Cox, T.; Witters, L.A.; Kemp, B.E.
Mammalian AMP-activated protein kinase subfamily
J. Biol. Chem.
271
611-614
1996
Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Beg, Z.H.; Stonik, J.A.; Brewer, H.B.
3-Hydroxy-3-methylglutaryl coenzyme A reductase: regulation of enzymatic activity by phosphorylation and dephosphorylation
Proc. Natl. Acad. Sci. USA
75
3678-3682
1978
Rattus norvegicus
Manually annotated by BRENDA team
Ingebritsen, T.S.; Lee, H.S.; Parker, R.A.; Gibson, D.M.
Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation
Biochem. Biophys. Res. Commun.
81
1268-1277
1978
Rattus norvegicus
Manually annotated by BRENDA team
Beg, Z.H.; Stonik, J.A.
Reversible inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase: reductase kinase and mevalonate kinase are separate enzymes
Biochem. Biophys. Res. Commun.
108
559-566
1982
Rattus norvegicus
Manually annotated by BRENDA team
Ferrer, A.; Hegardt, F.G.
Phosphorylation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
Arch. Biochem. Biophys.
230
227-237
1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Harwood, H.J.; Brandt, K.G.; Rodwell, V.W.
Allosteric activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by nucleoside diphosphates
J. Biol. Chem.
259
2810-2815
1984
Rattus norvegicus
Manually annotated by BRENDA team
Ferrer, A.; Caelles, C.; Massot, N.; Hegardt, F.G.
Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5-monophosphate
Biochem. Biophys. Res. Commun.
132
497-504
1985
Rattus norvegicus
Manually annotated by BRENDA team
Beg, Z.H.; Stonik, J.A.; Brewer, H.B.
Phosphorylation and modulation of the enzymic activity of native and protease-cleaved purified hepatic 3-hydroxy-3-methylglutaryl-coenzyme A reductase by a calcium/calmodulin-dependent protein kinase
J. Biol. Chem.
262
13228-13240
1987
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Ferrer, A.; Caelles, C.; Massot, N.; Hegardt, F.G.
Allosteric activation of rat liver microsomal [hydroxymethylglutaryl-CoA reductase (NADPH)]kinase by nucleoside phosphates
Biol. Chem. Hoppe-Seyler
368
249-257
1987
Rattus norvegicus
Manually annotated by BRENDA team
Weekes, J.; Ball, K.L.; Caudwell, F.B.; Hardie, D.G.
Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides
FEBS Lett.
334
335-339
1993
Brassica oleracea, Rattus norvegicus
Manually annotated by BRENDA team
Omkumar, R.V.; Darnay, B.G.; Rodwell, V.W.
Modulation of syrian hamster 3-hydroxy-3-methylglutaryl-CoA reductase activity by phosphorylation. Role of serine 871 [published erratum appears in J Biol Chem 1994 Jun 10;269(23):16518]
J. Biol. Chem.
269
6810-6814
1994
Rattus norvegicus
Manually annotated by BRENDA team
Henin, N.; Vincent, M.F.; Van den Berghe, G.
Stimulation of rat liver AMP-activated protein kinase by AMP analogues
Biochim. Biophys. Acta
1290
197-203
1996
Rattus norvegicus
Manually annotated by BRENDA team
Park, H.; Kaushik, V.K.; Constant, S.; Prentki, M.; Przybytkowski, E.; Ruderman, N.B.; Saha, A.K.
Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise
J. Biol. Chem.
277
32571-32577
2002
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Beg, Z.H.; Stonik, J.A.; Brewer, B.
Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Proc. Natl. Acad. Sci. USA
76
4375-4379
1979
Rattus norvegicus
Manually annotated by BRENDA team
Weekes, J.; Hawley, S.A.; Corton, J.; Shugar, D.; Hardie, D.G.
Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues
Eur. J. Biochem.
219
751-757
1994
Rattus norvegicus
Manually annotated by BRENDA team
Beg, Z.H.; Stonik, J.A.; Brewer, B.
In vivo modulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase, reductase kinase, and reductase kinase kinase by mevalonolactone
Proc. Natl. Acad. Sci. USA
81
7293-7297
1984
Rattus norvegicus
Manually annotated by BRENDA team
Hawley, S.A.; Selbert, M.A.; Goldstein, E.G.; Edelman, A.M.; Carling, D.; Hardie, D.G.
5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
J. Biol. Chem.
270
27186-27191
1995
Rattus norvegicus
Manually annotated by BRENDA team
Hawley, S.A.; Davison, M.; Woods, A.; Davies, S.P.; Beri, R.K.; Carling, D.; Hardie, D.G.
Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase
J. Biol. Chem.
271
27879-27887
1996
Rattus norvegicus
Manually annotated by BRENDA team
Woods, A.; Cheung, P.C.; Smith, F.C.; Davison, M.D.; Scott, J.; Beri, R.K.; Carling, D.
Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro
J. Biol. Chem.
271
10282-10290
1996
Rattus norvegicus
Manually annotated by BRENDA team
Crute, B.E.; Seefeld, K.; Gamble, J.; Kemp, B.E.; Witters, L.A.
Functional domains of the a1 catalytic subunit of the AMP-activated protein kinase
J. Biol. Chem.
273
35347-35354
1998
Rattus norvegicus
Manually annotated by BRENDA team
Muoio, D.M.; Seefeld, K.; Witters, L.A.; Coleman, R.A.
AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target
Biochem. J.
338
783-791
1999
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Stein, S.C.; Woods, A.; Jones, N.A.; Davison, M.D.; Carling, D.
The regulation of AMP-activated protein kinase by phosphorylation
Biochem. J.
345
437-443
2000
Rattus norvegicus
-
Manually annotated by BRENDA team
Musi, N.; Hayashi, T.; Fujii, N.; Hirshman, M.F.; Witters, L.A.; Goodyear, L.J.
AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle
Am. J. Physiol.
280
E677-684
2001
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Woods, A.; Vertommen, D.; Neumann, D.; Tuerk, R.; Bayliss, J.; Schlattner, U.; Wallimann, T.; Carling, D.; Rider, M.H.
Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis
J. Biol. Chem.
278
28434-28442
2003
Rattus norvegicus
Manually annotated by BRENDA team
Samari, H.R.; Moeller, M.T.N.; Holden, L.; Asmyhr, T.; Seglen, P.O.
Stimulation of hepatocytic AMP-activated protein kinase by okadaic acid and other autophygy-suppressive toxins
Biochem. J.
386
237-244
2005
Rattus norvegicus
Manually annotated by BRENDA team
Crawford, R.M.; Treharne, K.J.; Best, O.G.; Muimo, R.; Riemen, C.E.; Mehta, A
A novel physical and functional association between nucleoside diphosphate kinase A and AMP-activated protein kinase alpha1 in liver and lung
Biochem. J.
392
201-209
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Mukhtar, M.H.; Payne, V.A.; Arden, C.; Harbottle, A.; Khan, S.; Lange, A.J.; Agius, L.
Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R766-R774
2008
Rattus norvegicus
Manually annotated by BRENDA team
Borger, D.R.; Gavrilescu, L.C.; Bucur, M.C.; Ivan, M.; Decaprio, J.A.
AMP-activated protein kinase is essential for survival in chronic hypoxia
Biochem. Biophys. Res. Commun.
370
230-234
2008
Rattus norvegicus
Manually annotated by BRENDA team
Garcia-Villafranca, J.; Guillen, A.; Castro, J.
Ethanol consumption impairs regulation of fatty acid metabolism by decreasing the activity of AMP-activated protein kinase in rat liver
Biochimie
90
460-466
2008
Rattus norvegicus
Manually annotated by BRENDA team
Kim, S.J.; Jung, J.Y.; Kim, H.W.; Park, T.
Anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue of rats
Biol. Pharm. Bull.
31
1415-1421
2008
Rattus norvegicus
Manually annotated by BRENDA team
Gybina, A.A.; Prohaska, J.R.
Copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum
Brain Res.
1204
69-76
2008
Rattus norvegicus
Manually annotated by BRENDA team
Witczak, C.A.; Sharoff, C.G.; Goodyear, L.J.
AMP-activated protein kinase in skeletal muscle: from structure and localization to its role as a master regulator of cellular metabolism
Cell. Mol. Life Sci.
65
3737-3755
2008
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
McCrimmon, R.J.; Shaw, M.; Fan, X.; Cheng, H.; Ding, Y.; Vella, M.C.; Zhou, L.; McNay, E.C.; Sherwin, R.S.
Key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
Diabetes
57
444-450
2008
Rattus norvegicus
Manually annotated by BRENDA team
Robertson, T.P.; Mustard, K.J.; Lewis, T.H.; Clark, J.H.; Wyatt, C.N.; Blanco, E.A.; Peers, C.; Hardie, D.G.; Evans, A.M.
AMP-activated protein kinase and hypoxic pulmonary vasoconstriction
Eur. J. Pharmacol.
595
39-43
2008
Rattus norvegicus
Manually annotated by BRENDA team
Christ-Crain, M.; Kola, B.; Lolli, F.; Fekete, C.; Seboek, D.; Wittmann, G.; Feltrin, D.; Igreja, S.C.; Ajodha, S.; Harvey-White, J.; Kunos, G.; Mueller, B.; Pralong, F.; Aubert, G.; Arnaldi, G.; Giacchetti, G.; Boscaro, M.; Grossman, A.B.; Korbonits, M.
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes: a novel mechanism in Cushings syndrome
FASEB J.
22
1672-1683
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Summermatter, S.; Mainieri, D.; Russell, A.P.; Seydoux, J.; Montani, J.P.; Buchala, A.; Solinas, G.; Dulloo, A.G.
Thrifty metabolism that favors fat storage after caloric restriction: a role for skeletal muscle phosphatidylinositol-3-kinase activity and AMP-activated protein kinase
FASEB J.
22
774-785
2008
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Ronnett, G.V.; Aja, S.
AMP-activated protein kinase in the brain
Int. J. Obes.
32
S42-S48
2008
Rattus norvegicus
Manually annotated by BRENDA team
Riek, U.; Scholz, R.; Konarev, P.; Rufer, A.; Suter, M.; Nazabal, A.; Ringler, P.; Chami, M.; Mueller, S.A.; Neumann, D.; Forstner, M.; Hennig, M.; Zenobi, R.; Engel, A.; Svergun, D.; Schlattner, U.; Wallimann, T.
Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding
J. Biol. Chem.
283
18331-18343
2008
Rattus norvegicus (P54645), Rattus norvegicus (P80385), Rattus norvegicus (P80386), Rattus norvegicus (Q09137)
Manually annotated by BRENDA team
Iseli, T.J.; Oakhill, J.S.; Bailey, M.F.; Wee, S.; Walter, M.; van Denderen, B.J.; Castelli, L.A.; Katsis, F.; Witters, L.A.; Stapleton, D.; Macaulay, S.L.; Michell, B.J.; Kemp, B.E.
AMP-activated protein kinase subunit interactions: beta1:gamma1 association requires beta1 Thr-263 and Tyr-267
J. Biol. Chem.
283
4799-4807
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Vadasz, I.; Dada, L.A.; Briva, A.; Trejo, H.E.; Welch, L.C.; Chen, J.; Toth, P.T.; Lecuona, E.; Witters, L.A.; Schumacker, P.T.; Chandel, N.S.; Seeger, W.; Sznajder, J.I.
AMP-activated protein kinase regulates CO2-induced alveolar epithelial dysfunction in rats and human cells by promoting Na,K-ATPase endocytosis
J. Clin. Invest.
118
752-762
2008
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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.
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kelly, M.; Gauthier, M.S.; Saha, A.K.; Ruderman, N.B.
Activation of AMP-activated protein kinase by interleukin-6 in rat skeletal muscle: association with changes in cAMP, energy state, and endogenous fuel mobilization
Diabetes
58
1953-1960
2009
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Meares, G.P.; Hughes, K.J.; Jaimes, K.F.; Salvatori, A.S.; Rhodes, C.J.; Corbett, J.A.
AMP-activated protein kinase attenuates nitric oxide-induced beta-cell death
J. Biol. Chem.
285
3191-3200
2010
Rattus norvegicus
Manually annotated by BRENDA team
Bendayan, M.; Londono, I.; Kemp, B.E.; Hardie, G.D.; Ruderman, N.; Prentki, M.
Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy
J. Histochem. Cytochem.
57
963-971
2009
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chen, L.; Jiao, Z.H.; Zheng, L.S.; Zhang, Y.Y.; Xie, S.T.; Wang, Z.X.; Wu, J.W.
Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
Nature
459
1146-1149
2009
Saccharomyces cerevisiae, Rattus norvegicus, Schizosaccharomyces pombe
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Mobbs, J.I.; Koay, A.; Di Paolo, A.; Bieri, M.; Petrie, E.J.; Gorman, M.A.; Doughty, L.; Parker, M.W.; Stapleton, D.I.; Griffin, M.D.; Gooley, P.R.
Determinants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinase
Biochem. J.
468
245-257
2015
Rattus norvegicus (P80386), Rattus norvegicus (Q9QZH4)
Manually annotated by BRENDA team
Gao, F.; Qian, Y.J.; Chen, F.H.; Zhu, H.B.
Comparative analysis of stimulation and binding characteristics of adenosine analogs to AMP-activated protein kinase
J. Asian Nat. Prod. Res.
21
916-927
2019
Rattus norvegicus
Manually annotated by BRENDA team
Moral-Sanz, J.; Mahmoud, A.; Ross, F.; Eldstrom, J.; Fedida, D.; Hardie, D.; Evans, A.
AMP-activated protein kinase inhibits Kv1.5 channel currents of pulmonary arterial myocytes in response to hypoxia and inhibition of mitochondrial oxidative phosphorylation
J. Physiol.
594
4901-4915
2016
Rattus norvegicus
Manually annotated by BRENDA team
Hermann, R.; Mestre Cordero, V.; Fernandez Pazos, M.; Reznik, F.; Velez, D.; Savino, E.; Marina Prendes, M.; Varela, A.
Differential effects of AMP-activated protein kinase in isolated rat atria subjected to simulated ischemia-reperfusion depending on the energetic substrates available
Pflugers Arch.
470
367-383
2018
Rattus norvegicus
Manually annotated by BRENDA team