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Information on EC 2.7.11.27 - [acetyl-CoA carboxylase] kinase
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EC Tree
2.7.11.27 [acetyl-CoA carboxylase] kinaseIUBMB Comments
Phosphorylates and inactivates EC 6.4.1.2, acetyl-CoA carboxylase, which can be dephosphorylated and reactivated by EC 3.1.3.17, [phosphorylase] phosphatase. The enzyme is more active towards the dimeric form of acetyl-CoA carboxylase than the polymeric form . Phosphorylates serine residues.
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Word Map
- 2.7.11.27
- aicar
- 5-aminoimidazole-4-carboxamide
-
monophosphate-activated
-
accbeta
-
ampk-dependent
The enzyme appears in viruses and cellular organisms
Synonyms
ampkalpha, camp-activated protein kinase, 5'-amp activated protein kinase, acetyl-coa carboxylase kinase, acetyl-coa carboxylase kinase-2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-AMP activated protein kinase
acetyl coenzyme A carboxylase kinase (phosphorylating)
-
-
-
-
acetyl-CoA carboxylase kinase
-
-
-
-
acetyl-CoA carboxylase kinase (cAMP-independent)
-
-
-
-
acetyl-CoA carboxylase kinase-2
-
-
-
-
acetyl-CoA carboxylase kinase-3 (AMP-activated)
-
-
-
-
acetyl-coenzyme A carboxylase kinase
-
-
-
-
ACK2
-
-
-
-
ACK3
-
-
-
-
AMP-activated protein kinase
AMPK
AMPKalpha
EC 2.7.1.111
-
-
formerly
-
EC 2.7.1.128
-
-
formerly
-
I-peptide kinase
-
highly specific for acetyl-CoA carboxylase, binds selectively to the dimeric form
additional information
AMPK
-
-
-
-
additional information
-
cAMP-dependent protein kinase identified, that phosphorylates and inactivates acetyl-CoA carboxylase in vitro, but appears not to be involved in regulation in vivo
additional information
-
phosphorylation by cAMP-dependent protein kinase has the same effect on acetyl-CoA carboxylase activity then phosphorylation with acetyl-CoA carboxylase kinase-2
additional information
-
phosphorylation by cAMP-dependent protein kinase has the same effect on acetyl-CoA carboxylase activity then phosphorylation with acetyl-CoA carboxylase kinase-2
additional information
-
two other cAMP-independent kinases found, that phosphorylate but do not effect acetyl-CoA carboxylase kinase activity
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[acetyl-CoA carboxylase] phosphotransferase
Phosphorylates and inactivates EC 6.4.1.2, acetyl-CoA carboxylase, which can be dephosphorylated and reactivated by EC 3.1.3.17, [phosphorylase] phosphatase. The enzyme is more active towards the dimeric form of acetyl-CoA carboxylase than the polymeric form [5]. Phosphorylates serine residues.
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CAS REGISTRY NUMBER
COMMENTARY
77000-06-7
-
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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 + phosphorylase kinase
ADP + (phosphorylase kinase) phosphate
-
poor substrate
-
-
?
ATP + pyruvate kinase L
ADP + (pyruvate kinase L) phosphate
-
very poor substrate
-
-
?
ATP + histone
ADP + phosphohistone
-
histone H1 and H2B, very high activity with histone H2B
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
AMPK causes phosphorylation and inhibition of acetyl-CoA carboxylase, which reduces the production of malonyl-CoA
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
AMPKalpha negatively regulates activity of acetyl-CoA carboxylase and hepatic lipid content
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
the enzyme can directly inactivate acetyl-CoA carboxylase through phosphorylation of Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
no increase in acetyl-CoA carboxylase activity
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
no increase in acetyl-CoA carboxylase activity
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates Ser77 and Ser1200
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inactivation of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
incorporates 0.6 mol phosphate per mol of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
incorporates 0.6 mol phosphate per mol of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
incorporates 1.5 mol phosphate per mol of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
incorporates 0.45 mol phosphate per mol of carboxylase
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
involved in insulin dependent regulation of acetyl-CoA carboxylase in vivo
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
acetyl-CoA carboxylase bound kinase involved in regulation in vivo
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
most likely candidate for acetyl-CoA carboxylase inactivation in vivo
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
ACK3 and not ACK2 appears to be responsible for acetyl-CoA carboxylase inactivation in lactating mammary gland
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
regulation of acetyl-CoA carboxylase in muscle at metabolic stress conditions
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
regulation of acetyl-CoA carboxylase in muscle at metabolic stress conditions
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
acetyl-CoA carboxylase from skeletal muscle is more potently inhibited by palmitoyl-CoA after having been phosphorylated by AMPK. This may contribute to low muscle malonyl-CoA values and increasing fatty acid oxidation rates during long-term exercise when plasma fatty acid concentrations are elevated
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
changes in activity of acetyl-CoA carboxylase could be coordinated by AMPK
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
covalent activation of heart AMP-activated protein kinase in response to physiological concentrations of long-chain fatty acids, activation by an unknown fatty acid-driven signalling process
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
the hypothalamic AMP-activated protein kinase/acetyl-CoA carboxylase, i.e. AMPK/ACC, pathway plays an important role in the control of food intake and energy expenditure, overview
-
-
?
additional information
?
-
-
no activity with phosphorylase b and 3-hydroxy-3-methylglutaryl-CoA reductase
-
-
?
additional information
?
-
-
leptin stimulates fatty acid oxidation via the phosphorylation of AMP-activated protein kinase and acetyl-CoA carboxylase. Obesity is associated with resistance to the effects of leptin, overview
-
-
?
additional information
?
-
-
the enzyme activity in liver is associated to insulin signal transduction, overview
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
AMPK causes phosphorylation and inhibition of acetyl-CoA carboxylase, which reduces the production of malonyl-CoA
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
AMPKalpha negatively regulates activity of acetyl-CoA carboxylase and hepatic lipid content
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
the enzyme can directly inactivate acetyl-CoA carboxylase through phosphorylation of Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
involved in insulin dependent regulation of acetyl-CoA carboxylase in vivo
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
acetyl-CoA carboxylase bound kinase involved in regulation in vivo
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
most likely candidate for acetyl-CoA carboxylase inactivation in vivo
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
ACK3 and not ACK2 appears to be responsible for acetyl-CoA carboxylase inactivation in lactating mammary gland
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
regulation of acetyl-CoA carboxylase in muscle at metabolic stress conditions
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
regulation of acetyl-CoA carboxylase in muscle at metabolic stress conditions
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
acetyl-CoA carboxylase from skeletal muscle is more potently inhibited by palmitoyl-CoA after having been phosphorylated by AMPK. This may contribute to low muscle malonyl-CoA values and increasing fatty acid oxidation rates during long-term exercise when plasma fatty acid concentrations are elevated
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
changes in activity of acetyl-CoA carboxylase could be coordinated by AMPK
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
covalent activation of heart AMP-activated protein kinase in response to physiological concentrations of long-chain fatty acids, activation by an unknown fatty acid-driven signalling process
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
the hypothalamic AMP-activated protein kinase/acetyl-CoA carboxylase, i.e. AMPK/ACC, pathway plays an important role in the control of food intake and energy expenditure, overview
-
-
?
additional information
?
-
-
leptin stimulates fatty acid oxidation via the phosphorylation of AMP-activated protein kinase and acetyl-CoA carboxylase. Obesity is associated with resistance to the effects of leptin, overview
-
-
?
additional information
?
-
-
the enzyme activity in liver is associated to insulin signal transduction, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
citrate
-
strong inhibitor of the hypothalamic and the hepatic enzyme after intracerebroventricular injection and during fasting, rats treated with citrate present improved insulin signal transduction in liver, skeletal muscle, and epididymal fat pad, overview, no influence on enzyme expression
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adiponectin
adiponectin increases the phosphorylation and activation of AMPK, it increases inactivated acetyl-CoA carboxylase (ACC), which has been phosphorylated by activated AMPK, and subsequently increases expression of agouti-related peptide (AgRP) mRNA
-
cAMP-dependent protein kinase
-
phosphorylates and activates carboxylase kinase
-
CTRP1 protein
activates AMP-activated protein kinase (AMPK), which inhibits acetyl-CoA carboxylase (ACC) through phosphorylation. CTRP1 has a direct effect on AMPK signaling, recombinant CTRP1 administration acutely stimulates muscle AMPKalpha and ACC phosphorylation in vivo
-
fructose
-
acetyl-CoA carboxylase phosphorylation by the enzyme increases significantly and concentration-dependently in fructose-treated HepG2 cells in the presence of placental lactogen
leptin
-
stimulates fatty acid oxidation via the phosphorylation of AMPK and acetyl-CoA carboxylase, the stimulation by leptin is muscle fibre type-dependent and fails in diet-induced obesity
-
CoA
-
required, activates exclusively activity towards acetyl-CoA carboxylase, Ka: 0.025 mM, binds to carboxylase not to kinase
additional information
-
AMPK is activated in response to metabolic stresses, such as hypoxia and ischemia, and the anti-diabetic drug metformin
-
additional information
-
covalent activation of heart AMP-activated protein kinase in response to physiological concentrations of long-chain fatty acids, activation by an unknown fatty acid-driven signalling process
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Ataxia
Divergence of cAMP signalling pathways mediating augmented nucleotide excision repair and pigment induction in melanocytes.
Carcinoma
Activation of peroxisome proliferator-activated receptor beta/delta induces lung cancer growth via peroxisome proliferator-activated receptor coactivator gamma-1alpha.
Carcinoma, Hepatocellular
Cell cycle regulation via p53 phosphorylation by a 5'-AMP activated protein kinase activator, 5-aminoimidazole- 4-carboxamide-1-beta-D-ribofuranoside, in a human hepatocellular carcinoma cell line.
Cysts
Activation of an AMP-activated protein kinase is involved in post-diapause development of Artemia franciscana encysted embryos.
Fatty Liver, Alcoholic
Protective effect of Codonopsis lanceolata root extract against alcoholic fatty liver in the rat.
Glioma
Glucose deprivation affects the expression of genes encoding cAMP-activated protein kinase and related proteins in U87 glioma cells in ERN1 dependent manner.
Hyperlipidemias
Increased hepatic lipogenesis in insulin resistance and type 2 diabetes is associated to AMPK signaling pathway upregulation in Psammomys obesus.
Infections
Expression of an active LKB1 complex in cardiac myocytes results in decreased protein synthesis associated with phenylephrine-induced hypertrophy.
Insulin Resistance
Ablation of AMP-activated protein kinase alpha1 and alpha2 from mouse pancreatic beta cells and RIP2.Cre neurons suppresses insulin release in vivo.
Insulin Resistance
Aging impairs insulin-stimulated glucose uptake in rat skeletal muscle via suppressing AMPKalpha.
Kidney Neoplasms
Birt-Hogg-Dubé syndrome: from gene discovery to molecularly targeted therapies.
Melanoma
Divergence of cAMP signalling pathways mediating augmented nucleotide excision repair and pigment induction in melanocytes.
Mitochondrial Diseases
Diverse cytopathologies in mitochondrial disease are caused by AMP-activated protein kinase signaling.
Obesity
The role of hypothalamic AMP-activated protein kinase in ovariectomy-induced obesity in rats.
Ovarian Neoplasms
Metformin attenuates ovarian cancer cell growth in an AMP- kinase dispensable manner.
Overnutrition
Maternal overnutrition suppresses the phosphorylation of 5'-AMP-activated protein kinase in liver, but not skeletal muscle, in the fetal and neonatal sheep.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
a mouse immortalized hypothalamic neuronal cell line
brenda
additional information
-
phosphorylated AMPK and phosphorylated acetyl-CoA carboxylase are mainly found in primary human tumor specimens
brenda
-
determination of levels of hypothalamic phosphorylation of AMPK
brenda
-
determination of levels of hypothalamic phosphorylation of AMPK
-
brenda
-
stimulation of AMPKalpha by leptin differs in tissue of lean and obese rats, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
AMP-activated protein kinase (AMPK) is an evolutionarily conserved serine/threonine protein kinase
malfunction
-
phosphorylated enzyme AMPK is involved in impaired glucose metabolism, that increases the risk for squamous cell carcinoma of the head and neck (SCCHN) in humans
metabolism
physiological function
additional information
-
AMPK is activated in response to metabolic stresses, such as hypoxia and ischemia, and the anti-diabetic drug metformin
metabolism
-
AMPK activation by metformin regulates acetyl-CoA carboxylase (ACC) activity by its phosphorylation. ACC is a rate-controlling enzyme for the synthesis of malonyl-CoA, which plays a critical role in the synthesis of fatty acids and the inhibition of mitochondrial fatty acid oxidation in the liver. the enzyme activator metformin decreases high-fat diet-induced renal injury by regulating the expression of adipokines and the renal AMP-activated protein kinase/acetyl-CoA carboxylase pathway in mice
metabolism
globular adiponectin regulates energy homeostasis through AMP-activated protein kinase-acetyl-CoA carboxylase (AMPK/ACC) pathway, but not the JAK/STAT3 pathway, in the hypothalamus. Adiponectin increases the phosphorylation and activation of AMPK, it increases inactivated acetyl-CoA carboxylase (ACC), which has been phosphorylated by activated AMPK, and subsequently increases expression of agouti-related peptide (AgRP) mRNA. Adiponectin had no effect on signal transducer and activator of transcription (STAT3), overview
metabolism
-
the reduction of hypothalamic acetyl-CoA carboxylase increases phophoenolpyruvate carboxykinase expression, AMPK phosphorylation, and glucose production in the liver. These effects are observed without modification of hypothalamic AMPK phosphorylation. Fasted rats show greater AMPK phosphorylation levels than fed rats. Reduced AMPK phosphorylation is linked to an increase in acetyl-CoA carboxylase activity and biosynthesis of malonyl-CoA
metabolism
-
AMPK activation by metformin regulates acetyl-CoA carboxylase (ACC) activity by its phosphorylation. ACC is a rate-controlling enzyme for the synthesis of malonyl-CoA, which plays a critical role in the synthesis of fatty acids and the inhibition of mitochondrial fatty acid oxidation in the liver. the enzyme activator metformin decreases high-fat diet-induced renal injury by regulating the expression of adipokines and the renal AMP-activated protein kinase/acetyl-CoA carboxylase pathway in mice
-
metabolism
-
the reduction of hypothalamic acetyl-CoA carboxylase increases phophoenolpyruvate carboxykinase expression, AMPK phosphorylation, and glucose production in the liver. These effects are observed without modification of hypothalamic AMPK phosphorylation. Fasted rats show greater AMPK phosphorylation levels than fed rats. Reduced AMPK phosphorylation is linked to an increase in acetyl-CoA carboxylase activity and biosynthesis of malonyl-CoA
-
physiological function
-
AMP-activated protein kinase (AMPK) regulates glucose and lipid metabolism via the phosphorylation and subsequent inactivation of its downstream target acetyl-CoA carboxylase (ACC). AMPK acts as a cellular fuel sensor by controlling intracellular energy levels to maintain appropriate cell growth rates. Phosphorylation and activation of AMPK stimulates fatty acid oxidation through the phosphorylation and subsequent inhibition of its downstream target acetyl-CoA carboxylase. Phosphorylated acetyl-CoA carboxylase may play a role in tumor progression of squamous cell carcinoma of the head and neck and may help to identify patient subgroups at high risk for poor disease outcome
physiological function
AMP-activated protein kinase (AMPK) represents an energy sensor that responds to hormone and nutrition status in vivo and exerts a regulatory effect in the hypothalamus and multiple peripheral tissues. AMP-activated protein inhibits acetyl-CoA carboxylase (ACC) through phosphorylation
physiological function
-
AMPK activation by metformin regulates acetyl-CoA carboxylase (ACC) activity by its phosphorylation. AMP-activated protein kinase (AMPK) is involved in the cellular metabolic response to metabolic stress. Metabolic stress, such as impaired ATP production or accelerated ATP consumption activate the AMP-activated protein kinase (AMPK) system, which acts as a sensor of cellular energy metabolism
physiological function
CTRP1 protein, a regulator of fatty acid metabolism, enhances fatty acid oxidation via AMP-activated protein kinase (AMPK) activation and acetyl-CoA carboxylase (ACC) inhibition
physiological function
-
hypothalamic AMPK acts as a cell energy sensor and can modulate food intake, glucose homeostasis, and fatty acid biosynthesis. Intrahypothalamic fatty acid injection is known to suppress liver glucose production, mainly by activation of hypothalamic ATP-sensitive potassium (K(ATP)) channels
physiological function
-
the enzyme is a central regulator of the energy status of the cell.The adipocyte enzyme is required for acute brown adipose tissue-mediated thermogenesis, the browning of white adipose tissue in response to beta3-adrenergic stimuli, and protection against the deleterious effects of a high fat diet via the regulation of the mitochondrial quality control pathway (mitophagy). The enzyme is not important for the glucose and lipid-lowering effects of fibroblast growth factor 21
physiological function
-
AMPK activation by metformin regulates acetyl-CoA carboxylase (ACC) activity by its phosphorylation. AMP-activated protein kinase (AMPK) is involved in the cellular metabolic response to metabolic stress. Metabolic stress, such as impaired ATP production or accelerated ATP consumption activate the AMP-activated protein kinase (AMPK) system, which acts as a sensor of cellular energy metabolism
-
physiological function
-
CTRP1 protein, a regulator of fatty acid metabolism, enhances fatty acid oxidation via AMP-activated protein kinase (AMPK) activation and acetyl-CoA carboxylase (ACC) inhibition
-
physiological function
-
hypothalamic AMPK acts as a cell energy sensor and can modulate food intake, glucose homeostasis, and fatty acid biosynthesis. Intrahypothalamic fatty acid injection is known to suppress liver glucose production, mainly by activation of hypothalamic ATP-sensitive potassium (K(ATP)) channels
-
Show AA Sequence and Transmembrane Helices (1571 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
76000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
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the enzyme is activated through phosphorylation by liver kinase B1
phosphoprotein
-
determination of levels of hypothalamic phosphorylation of AMPK
phosphoprotein
-
determination of levels of hypothalamic phosphorylation of AMPK
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 10 mM phosphate buffer, pH 7, 2 mM EDTA, 10 mM 2-mercaptoethanol, 20% glycerol, 4 weeks, no loss of activity
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-70°C, partially purified kinase preparation, stable for several months, highly purified kinase is very labile and loses activity within 5 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
-
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
recombinant CTRP1 acutely induces AMPKalpha and ACC phosphorylation in skeletal muscle
recombinant CTRP1 acutely induces AMPKalpha and ACC phosphorylation in skeletal muscle
recombinant CTRP1 acutely induces AMPKalpha and ACC phosphorylation in skeletal muscle
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
strong expression of phosphorylated acetyl-CoA carboxylase is an independent prognostic marker for patients with nodepositive of squamous cell carcinoma of the head and neck
medicine
medicine
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clinical application of the enzyme activator metformin to obese or early diabetic patients may be helpful in preventing obesity- or diabetes-related kidney disease
medicine
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clinical application of the enzyme activator metformin to obese or early diabetic patients may be helpful in preventing obesity- or diabetes-related kidney disease
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shiao, M.S.; Drong, R.F.; Porter, J.W.
The purification and properties of a protein kinase and the partial purification of a phosphoprotein phosphatase that inactivate and activate acetyl-CoA carboxylase
Biochem. Biophys. Res. Commun.
98
80-87
1981
Rattus norvegicus
brenda
Jamil, H.; Madsen, N.B.
Phosphorylation state of acetyl-coenzyme A carboxylase. I. Linear inverse relationship to activity ratios at different citrate concentrations
J. Biol. Chem.
262
630-637
1987
Rattus norvegicus
brenda
Lent, B.A.; Kim, K.H.
Purification and properties of a kinase which phosphorylates and inactivates acetyl-CoA carboxylase
J. Biol. Chem.
257
1897-1901
1982
Rattus norvegicus
brenda
Lent, B.A.; Kim, K.H.
Requirement of acetyl-coenzyme A carboxylase kinase for coenzyme A
Arch. Biochem. Biophys.
225
964-971
1983
Rattus norvegicus
brenda
Lent, B.A.; Kim, K.H.
Phosphorylation and activation of acetyl-coenzyme A Carboxylase kinase by the catalytic subunit of cyclic AMP-dependent protein kinase
Arch. Biochem. Biophys.
225
972-978
1983
Rattus norvegicus
brenda
Munday, M.R.; Hardie, D.G.
Isolation of three cyclic-AMP-independent acetyl-CoA carboxylase kinases from lactating rat mammary gland and characterization of their effects on enzyme activity
Eur. J. Biochem.
141
617-627
1984
Rattus norvegicus
brenda
Munday, M.R.; Campbell, D.G.; Carling, D.; Hardie, D.G.
Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase
Eur. J. Biochem.
175
331-338
1988
Rattus norvegicus
brenda
Ottey, K.A.; Takhar, S.; Munday, M.R.
Comparison of two cyclic-nucleotide-independent acetyl-CoA carboxylase kinase from lactating rat mammary gland: identification of the kinase responsible for acetyl-CoA inactivation in vivo
Biochem. Soc. Trans.
17
349-350
1989
Rattus norvegicus
-
brenda
Ottey, K.A.; Munday, M.R.; Calvert, D.T.; Clegg, R.A.
Effect of anoxia on acetyl-CoA carboxylase activity: possible role for an AMP-activated protein kinase
Biochem. Soc. Trans.
17
350-351
1989
Rattus norvegicus
-
brenda
Mohamed, A.H.; Huang, W.Y.; Huang, W.; Venkatachalam, K.V.; Wakil, S.J.
Isolation and characterization of a novel acetyl-CoA carboxylase kinase from rat liver
J. Biol. Chem.
269
6859-6865
1994
Rattus norvegicus
brenda
Heesom, K.J.; Moule, S.K.; Denton, R.M.
Purification of an insulin-stimulated acetyl-CoA carboxylase kinase from rat epididymal adipose tissue
Biochem. Soc. Trans.
23
180S
1995
Rattus norvegicus
brenda
Vavvas, D.; Apazidis, A.; Saha, A.K.; Gamble, J.; Patel, A.; Kemp, B.E.; Witters, L.A.; Ruderman, N.B.
Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle
J. Biol. Chem.
272
13255-13261
1997
Rattus norvegicus
brenda
Gamble, J.; Lopaschuk, G.D.
Insulin inhibition of 5' adenosine monophosphate-activated protein kinase in the heart results in activation of acetyl coenzyme A carboxylase and inhibition of fatty acid oxidation
Metabolism
46
1270-1274
1997
Rattus norvegicus
brenda
Heesom, K.J.; Moule, S.K.; Denton, R.M.
Purification and characterisation of an insulin-stimulated protein-serine kinase which phosphorylates acetyl-CoA carboxylase
FEBS Lett.
422
43-46
1998
Rattus norvegicus
brenda
Hopkins, T.A.; Dyck, J.R.B.; Lopaschuk, G.D.
AMP-activated protein kinase regulation of fatty acid oxidation in the ischaemic heart
Biochem. Soc. Trans.
31
207-212
2003
Homo sapiens
brenda
Wojtaszewski, J.F.; MacDonald, C.; Nielsen, J.N.; Hellsten, Y.; Hardie, D.G.; Kemp, B.E.; Kiens, B.; Richter, E.A.
Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle
Am. J. Physiol.
284
E813-822
2003
Homo sapiens
brenda
Assifi, M.M.; Suchankova, G.; Constant, S.; Prentki, M.; Saha, A.K.; Ruderman, N.B.
AMP-activated protein kinase and coordination of hepatic fatty acid metabolism of starved/carbohydrate-refed rats
Am. J. Physiol.
289
E794-800
2005
Rattus norvegicus
brenda
Horman, S.; Hussain, N.; Dilworth, S.M.; Storey, K.B.; Rider, M.H.
Evaluation of the role of AMP-activated protein kinase and its downstream targets in mammalian hibernation
Comp. Biochem. Physiol. B
142
374-382
2005
Ictidomys tridecemlineatus
brenda
Clark, H.; Carling, D.; Saggerson, D.
Covalent activation of heart AMP-activated protein kinase in response to physiological concentrations of long-chain fatty acids
Eur. J. Biochem.
271
2215-2224
2004
Rattus norvegicus
brenda
Rubink, D.S.; Winder, W.W.
Effect of phosphorylation by AMP-activated protein kinase on palmitoyl-CoA inhibition of skeletal muscle acetyl-CoA carboxylase
J. Appl. Physiol.
98
1221-1227
2005
Rattus norvegicus
brenda
Zang, M.; Zuccollo, A.; Hou, X.; Nagata, D.; Walsh, K.; Herscovitz, H.; Brecher, P.; Ruderman, N.B.; Cohen, R.A.
AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulin-resistant human HepG2 cells
J. Biol. Chem.
279
47898-47905
2004
Homo sapiens
brenda
Cesquini, M.; Stoppa, G.R.; Prada, P.O.; Torsoni, A.S.; Romanatto, T.; Souza, A.; Saad, M.J.; Velloso, L.A.; Torsoni, M.A.
Citrate diminishes hypothalamic acetyl-CoA carboxylase phosphorylation and modulates satiety signals and hepatic mechanisms involved in glucose homeostasis in rats
Life Sci.
82
1262-1271
2008
Rattus norvegicus
brenda
Janovska, A.; Hatzinikolas, G.; Staikopoulos, V.; McInerney, J.; Mano, M.; Wittert, G.A.
AMPK and ACC phosphorylation: effect of leptin, muscle fibre type and obesity
Mol. Cell. Endocrinol.
284
1-10
2008
Rattus norvegicus
brenda
Kim, D.; Lee, J.E.; Jung, Y.J.; Lee, A.S.; Lee, S.; Park, S.K.; Kim, S.H.; Park, B.H.; Kim, W.; Kang, K.P.
Metformin decreases high-fat diet-induced renal injury by regulating the expression of adipokines and the renal AMP-activated protein kinase/acetyl-CoA carboxylase pathway in mice
Int. J. Mol. Med.
32
1293-1302
2013
Mus musculus, Mus musculus C57BL/6
brenda
Peterson, J.M.; Aja, S.; Wei, Z.; Wong, G.W.
CTRP1 protein enhances fatty acid oxidation via AMP-activated protein kinase (AMPK) activation and acetyl-CoA carboxylase (ACC) inhibition
J. Biol. Chem.
287
1576-1587
2012
Mus musculus (Q5EG47 AND Q8BRK8), Mus musculus C57BL/6 (Q5EG47 AND Q8BRK8)
brenda
Wen, J.P.; Liu, C.E.; Hu, Y.T.; Chen, G.; Lin, L.X.
Globular adiponectin regulates energy homeostasis through AMP-activated protein kinase-acetyl-CoA carboxylase (AMPK/ACC) pathway in the hypothalamus
Mol. Cell. Biochem.
344
109-115
2010
Mus musculus (Q5EG47 AND Q8BRK8)
brenda
Santos, G.A.; Pereira, V.D.; Roman, E.A.; Ignacio-Souza, L.; Vitorino, D.C.; de Moura, R.F.; Razolli, D.S.; Torsoni, A.S.; Velloso, L.A.; Torsoni, M.A.
Hypothalamic inhibition of acetyl-CoA carboxylase stimulates hepatic counter-regulatory response independent of AMPK activation in rats
PLoS ONE
8
e62669
2013
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Su, Y.W.; Lin, Y.H.; Pai, M.H.; Lo, A.C.; Lee, Y.C.; Fang, I.C.; Lin, J.; Hsieh, R.K.; Chang, Y.F.; Chen, C.L.
Association between phosphorylated AMP-activated protein kinase and acetyl-CoA carboxylase expression and outcome in patients with squamous cell carcinoma of the head and neck
PLoS ONE
9
e96183
2014
Homo sapiens
brenda
Mukai, Y.; Hoshi, F.; Sato, S.
Effect of fructose on the phosphorylation of AMP-activated protein kinase and acetyl-CoA carboxylase in HepG2 cells stimulated with placental lactogen
Birth Defects Res. B Dev. Reprod. Toxicol.
107
206-210
2016
Homo sapiens
brenda
Mottillo, E.P.; Desjardins, E.M.; Fritzen, A.M.; Zou, V.Z.; Crane, J.D.; Yabut, J.M.; Kiens, B.; Erion, D.M.; Lanba, A.; Granneman, J.G.; Talukdar, S.; Steinberg, G.R.
FGF21 does not require adipocyte AMP-activated protein kinase (AMPK) or the phosphorylation of acetyl-CoA carboxylase (ACC) to mediate improvements in whole-body glucose homeostasis
Mol. Metab.
6
471-481
2017
Mus musculus
brenda
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EXTERNAL LINKS (specific for EC-Number 2.7.11.27)
Transporter Classification Database (TCDB): 8.A.104.1.1
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