Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.11.27 - [acetyl-CoA carboxylase] kinase and Organism(s) Homo sapiens

for references in articles please use BRENDA:EC2.7.11.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB 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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected 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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
-
-
AMPKalpha
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
77000-06-7
-
SUBSTRATE
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]
ADP + [acetyl-CoA carboxylase] phosphate
show the reaction diagram
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]
ADP + [acetyl-CoA carboxylase] phosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
fructose
-
acetyl-CoA carboxylase phosphorylation by the enzyme increases significantly and concentration-dependently in fructose-treated HepG2 cells in the presence of placental lactogen
additional information
-
AMPK is activated in response to metabolic stresses, such as hypoxia and ischemia, and the anti-diabetic drug metformin
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
phosphorylated AMPK and phosphorylated acetyl-CoA carboxylase are mainly found in primary human tumor specimens
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in primary human tumor specimens
Manually annotated by BRENDA team
-
in healthy mucosa tissue
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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
additional information
-
AMPK is activated in response to metabolic stresses, such as hypoxia and ischemia, and the anti-diabetic drug metformin
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AAPK1_HUMAN
559
0
64009
Swiss-Prot
other Location (Reliability: 4)
AAPK2_HUMAN
552
0
62320
Swiss-Prot
other Location (Reliability: 1)
A0MZF5_HUMAN
552
0
62306
TrEMBL
other Location (Reliability: 1)
B2RA25_HUMAN
552
0
62330
TrEMBL
other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
-
the enzyme is activated through phosphorylation by liver kinase B1
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team