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Information on EC 6.4.1.2 - acetyl-CoA carboxylase and Organism(s) Rattus norvegicus and UniProt Accession P11497
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6.4.1.2 acetyl-CoA carboxylaseIUBMB Comments
This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
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Word Map
- 6.4.1.2
-
amp-activated
- triglyceride
-
lipogenesis
- adipose
-
lipogenic
- sterol
- peroxisome
- cholesterol
- obesity
- carnitine
- malonyl-coa
-
proliferator-activated
-
high-fat
- adipocytes
- lipoprotein
-
element-binding
- biotin
- steatosis
- lipase
-
obese
-
herbicide
- srebp-1c
- triacylglycerols
-
diet-induced
- stearoyl-coa
-
malic
- adiponectin
- nafld
-
lipolysis
-
monophosphate-activated
-
hfd-induced
- protein-1c
-
weed
- carboxylases
- aicar
-
atp-citrate
-
malonyl
-
desaturase-1
-
anti-obesity
-
biotin-dependent
-
hormone-sensitive
-
chrebp
-
5'-amp-activated
-
palmitoyltransferase-1
-
target-site
- adenoid
-
srebf1
-
anti-adipogenic
- lolium
- biotechnology
- medicine
-
herbicide-resistant
- pharmacology
- synthesis
- drug development
- biofuel production
- agriculture
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acetyl-coa carboxylase, accase, acetyl coa carboxylase, acetyl-coenzyme a carboxylase, acaca, acc-2, acetyl coenzyme a carboxylase, acetyl-coa carboxylase 1, acc-1, acacb, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACC
ACC1
ACC2
ACCase
-
-
-
-
Acetyl CoA carboxylase
Acetyl coenzyme A carboxylase
-
-
-
-
Acetyl-coenzyme A carboxylase
-
-
-
-
Carboxylase, acetyl coenzyme A
-
-
-
-
additional information
Acetyl CoA carboxylase
-
-
-
-
additional information
the enzyme belongs to the family of biotin-dependent carboxylases
additional information
-
the enzyme belongs to the family of biotin-dependent carboxylases
additional information
the enzyme belongs to the family of biotin-dependent carboxylases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
ordered bi bi uni uni ping-pong mechanism
-
ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
two-step reaction mechanism, structure-activity relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:hydrogencarbonate ligase (ADP-forming)
This enzyme is a multi-domain polypeptide that catalyses three different activities - a biotin carboxyl-carrier protein (BCCP), a biotin carboxylase that catalyses the transfer of a carboxyl group from hydrogencarbonate to the biotin molecule carried by the carrier protein, and the transfer of the carboxyl group from biotin to acetyl-CoA, forming malonyl-CoA. In some organisms these activities are catalysed by separate enzymes (see EC 6.3.4.14, biotin carboxylase, and EC 2.1.3.15, acetyl-CoA carboxytransferase). The carboxylation of the carrier protein requires ATP, while the transfer of the carboxyl group to acetyl-CoA does not.
CAS REGISTRY NUMBER
COMMENTARY
9023-93-2
-
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
additional information
?
-
-
perinatal copper deficiency in rat pups inhibits the enzyme, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
first committed step in fatty acid biosynthesis, hormonal, nutrient, and tissue-specific regulation of ACC genes, regulation of isozyme activity, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
first committed step in fatty acid biosynthesis, hormonal, nutrient, and tissue-specific regulation of ACC genes, regulation of isozyme activity, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first step in fatty acid biosynthesis
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
isozyme Acc1 catalyzes the committed and rate-determining step in the biosynthesis of long-chain fatty acids, while isozyme Acc2 produces a potent inhibitor of fatty acid oxidation, biological functions
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis, involved in regulation of fatty acid uptake into mitochondria
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis, key regulator of muscle fatty acid oxidation
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
first enzyme in fatty acid biosynthesis, regulated by AMP-activated protein kinase, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
intracellular citrate controls ACC activity and malonyl-CoA levels, and diminishes food intake, physiological regulation system involving citrate, overview
-
-
?
ATP + propionyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
-
maximal rate is 20% of that for acetyl-CoA
-
-
?
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 + HCO3-
ADP + malonyl-CoA + phosphate
first committed step in fatty acid biosynthesis, hormonal, nutrient, and tissue-specific regulation of ACC genes, regulation of isozyme activity, overview
-
-
?
additional information
?
-
-
perinatal copper deficiency in rat pups inhibits the enzyme, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
first committed step in fatty acid biosynthesis, hormonal, nutrient, and tissue-specific regulation of ACC genes, regulation of isozyme activity, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first step in fatty acid biosynthesis
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
isozyme Acc1 catalyzes the committed and rate-determining step in the biosynthesis of long-chain fatty acids, while isozyme Acc2 produces a potent inhibitor of fatty acid oxidation, biological functions
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis, involved in regulation of fatty acid uptake into mitochondria
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis, key regulator of muscle fatty acid oxidation
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
first enzyme in fatty acid biosynthesis, regulated by AMP-activated protein kinase, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
intracellular citrate controls ACC activity and malonyl-CoA levels, and diminishes food intake, physiological regulation system involving citrate, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
phosphate
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
phosphate
-
phosphate content of the 10000000 MW enzyme form: 4.0 mol of phosphate per mol of subunit. Phosphate content of the 2000000 MW enzyme form: 6.0 mol phosphate per mol of subunit. The 10000000 MW subunit and the 2000000 MW subunit are interconvertible by phosphorylation and dephosphorylation. Dephosphorylation by [acetyl-CoA carboxylase]-phosphatase 2 activates the enzyme and reduces its dependence on citrate
phosphate
-
contains approximately 6 mol phosphate per 240000 g of protein
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-(tetradecyloxy)-2-furoic acid
an ACC1 inhibitor e.g. in beta cells
(2-[(1E,3Z)-hexa-1,3,5-trien-1-yl]quinolin-4-yl)(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)methanone
-
-
(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)(quinolin-4-yl)methanone
-
-
(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)[3-(1H-pyrazol-3-yl)phenyl]methanone
-
-
(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)[3-(1H-pyrazol-4-yl)phenyl]methanone
-
-
1'-(1H-indazol-7-ylcarbonyl)-5-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-6,7-dimethylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-6,8-dimethylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-6-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-6-methylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-7-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-7-methylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-(1H-indazol-7-ylcarbonyl)-7-phenylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidine]-6-carboxylic acid
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1-methyl-1H-pyrazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1-methyl-1H-pyrazol-4-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1H-pyrazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1H-pyrazol-4-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(2-methyl-1,3-oxazol-4-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(2-methyl-1,3-oxazol-5-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(5-methyl-1H-pyrazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1-[(3,7-dimethyl-1H-indazol-5-yl)carbonyl]-5'-(propan-2-yloxy)spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
1-[(3,7-dimethyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
-
-
1-[(3-methyl-1H-indazol-5-yl)carbonyl]-5'-(propan-2-yloxy)spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
1-[(3-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
-
-
1-[(7-methyl-1H-indazol-5-yl)carbonyl]-5'-(propan-2-yloxy)spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
1-[(7-methyl-1H-indazol-5-yl)carbonyl]-6'-(1-methyl-1H-pyrazol-4-yl)spiro[piperidine-4,2'-pyrano[2,3-c]pyridin]-4'(3'H)-one
-
-
1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
-
-
1H-indazol-7-yl(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)methanone
-
-
2,2-dimethylpropyl [[trans-4-([[(2-[4-[2-(dimethylamino)ethyl]piperidin-1-yl]quinolin-4-yl)-carbonyl]amino]-methyl)cyclohexyl]methyl]carbamate
-
-
4-(4-[[(trans-4-[[(tert-butoxycarbonyl)amino]methyl]-cyclohexyl)methyl]carbamoyl]quinolin-2-yl)benzoic acid
-
-
5'-(butan-2-yloxy)-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
5'-ethoxy-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
5'-methoxy-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
5'-methoxy-7'-methyl-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
-
-
5-methoxy-1'-([2-(1-methyl-1H-pyrazol-3-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-methoxy-1'-([2-(pyridazin-4-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-methoxy-1'-([2-(pyridin-2-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-methoxy-1'-([2-(pyridin-3-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-methoxy-1'-([2-(pyridin-4-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-methoxy-1'-[(2-phenyl-1H-benzimidazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-methoxy-1'-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
5-[(5-methoxy-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)carbonyl]-1H-indole-2-carboxamide
-
-
5-[(5-methoxy-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)carbonyl]-N-methyl-1H-indole-2-carboxamide
-
-
5-[4-[(4-[1-[(1-acetylpiperidin-4-yl)carbonyl]piperidin-4-yl]piperazin-1-yl)carbonyl]-6-phenylpyridin-2-yl]-2-methyl-1H-indole-3-carbonitrile
-
-
6'-(1-methyl-1H-pyrazol-4-yl)-1-([2-(1-methyl-1H-pyrazol-3-yl)-1H-benzimidazol-6-yl]carbonyl)spiro[piperidine-4,2'-pyrano[2,3-c]pyridin]-4'(3'H)-one
-
-
6'-amino-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
-
-
6'-methoxy-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[2,3-c]pyridin]-4'(3'H)-one
-
-
6'-methyl-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
-
-
6,7-dimethyl-1'-[(3-methyl-1H-indazol-6-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
6,7-dimethyl-1'-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
6-(3,5-dimethyl-1,2-oxazol-4-yl)-1'-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
6-chloro-1'-(1H-indazol-7-ylcarbonyl)-5-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
6-chloro-1'-(1H-indazol-7-ylcarbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
anthracen-9-yl(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)methanone
-
-
beta,beta'-Tetramethyl-substituted hexadecanedioic acid
-
i.e. MEDICA, dead-end inhibitor
ethyl [[trans-4-([[(2-[4-[2-(dimethylamino)ethyl]-piperidin-1-yl]quinolin-4-yl)carbonyl]-amino]methyl)cyclo-hexyl]-methyl]carbamate
-
-
High molecular weight protein
-
from rat liver cytosol, approximately 1500000-2000000 Da
-
N-[(R)-3-[4-(6-isopropoxy-pyridin-3-yloxy)-phenyl]-1-methyl-propyl]-acetamide
-
submicromolar dualACC1/2 inhibitor
N-[(S)-3-[4-(6-isopropoxy-pyridin-3-yloxy)-phenyl]-1-methyl-propyl]-acetamide
-
submicromolar dualACC1/2 inhibitor
soraphen A
-
macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain
tert-butyl ([trans-4-[([[2-(3,5-dimethylisoxazol-4-yl)-quinolin-4-yl]carbonyl]amino)-methyl]cyclohexyl]methyl)carbamate
-
-
tert-butyl ([trans-4-[([[2-(4-[2-[(2-methoxyethyl)-amino]ethyl]piperidin-1-yl)quinolin-4-yl]carbonyl]amino)-methyl]cyclohexyl]methyl)carbamate
-
-
tert-butyl [(4-[[(naphthalen-2-ylsulfonyl)amino]methyl]cyclohexyl)methyl]carbamate
-
-
tert-butyl [(trans-4-((6-phenyl-1H-pyrrolo[2,3-b]-pyridine-4-carboxamido)methyl)cyclohexyl]methyl)carbamate
-
-
tert-butyl [(trans-4-[([[2-(1H-pyrazol-4-yl)quinolin-4-yl]-carbonyl]amino)methyl]cyclohexyl]methyl)carbamate
-
-
tert-butyl [(trans-4-[[(2-methyl-6-phenylisonicotinoyl)-amino]methyl]cyclohexyl)methyl]carbamate
-
-
tert-butyl [(trans-4-[[(2-phenylisonicotinoyl)amino]-methyl]cyclohexyl)methyl]carbamate
-
-
tert-butyl [(trans-4-[[([2-[4-(2-aminoethyl)piperidin-1-yl]quinolin-4-yl]carbonyl)amino]methyl]cyclohexyl)methyl]carbamate
-
-
tert-butyl [(trans-4-[[([2-[4-(2-hydroxyethyl)piperazin-1-yl]quinolin-4-yl]carbonyl)amino]-methyl]cyclohexyl)methyl]-carbamate
-
-
tert-butyl [(trans-4-[[([2-[4-(2-hydroxyethyl)piperidin-1-yl]quinolin-4-yl]carbonyl)amino]-methyl]cyclohexyl)-methyl]carbamate
-
-
tert-butyl [(trans-4-[[([2-[4-(aminomethyl)piperidin-1-yl]quinolin-4-yl]carbonyl)amino]methyl]-cyclohexyl)methyl]carbamate
-
-
tert-butyl [[cis-4-([[(2-phenylquinolin-4-yl)carbonyl]-amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-(piperazin-1-yl)quinolin-4-yl)-carbonyl]amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-chloroquinolin-4-yl)carbonyl]-amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-phenylquinolin-4-yl)carbonyl]-amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-phenylquinolin-4-yl)sulfonothioyl]amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-pyridin-4-ylquinolin-4-yl)carbonyl]amino]methyl)-cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-[1-[2-(dimethylamino)ethyl]-1H-pyrazol-4-yl]quinolin-4-yl)carbonyl]-amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-[3-(aminomethyl)phenyl]-quinolin-4-yl)carbonyl]amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-[3-[2-(dimethylamino)ethoxy]-azetidin-1-yl]-quinolin-4-yl)carbonyl]-amino]methyl)cyclohexyl]methyl]carbamate
-
-
tert-butyl [[trans-4-([[(2-[4-(aminomethyl)phenyl]quinolin-4-yl)carbonyl]amino]methyl)cyclo-hexyl]methyl]carbamate acetate
-
-
tert-butyl [[trans-4-([[(2-[4-[2-(dimethylamino)ethyl]-piperidin-1-yl]quinolin-4-yl)carbonyl]-amino]methyl)cyclohexyl]-methyl]carbamate
-
-
tetrahydro-2H-pyran-4-yl [[trans-4-([[(2-[4-[2-(di-methylamino)ethyl]piperidin-1-yl]quinolin-4-yl)carbonyl]-amino]-methyl)cyclohexyl]methyl]carbamate
-
-
[4-(1,3-benzodioxol-5-ylmethyl)piperazin-1-yl](2-phenylquinolin-4-yl)methanone
-
-
[trans-4-([[(2-[4-[2-(dimethylamino)ethyl]piperidin-1-yl]quinolin-4-yl)carbonyl]amino]methyl)-cyclohexyl]methyltert-butylcarbamate
-
-
CoA
-
inhibition requires the presence of MgATP2-, but is independent of phosphorylation of the enzyme, the effect is complete in about 5 min and is associated with depolymerization of acetyl-CoA carboxylase, half-maximal inhibition at 0.04 mM CoA, inhibition is partially reversed by incubation with citrate and more fully overcome by treatment of the enzyme with the insulin-stimulated acetyl-CoA carboxylase
additional information
-
3,3,14,14-tetramethylhexanedecadienoic acid treatment if animals inhibits activity in liver by activation of AMP-activated protein kinase, no effect in muscle
-
additional information
-
no inhibition of the rat enzyme by pyrrolidine dione moiramide B, i.e. (2E,4E)-hexa-2,4-dienoic acid [(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-amide, and its derivatve 6-fluoro-pyridine-2-carboxylic acid [(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-amide
-
additional information
-
phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, FOP herbicides are weak inhibitors of the rat enzyme
-
additional information
-
activated AMP-activated protein kinase, AMPK, phosphorylates and inhibits acetyl-CoA carboxylase. ACC is inhibited in Cu-deficient cerebella
-
additional information
-
an ethanol extract of Polygonum hypoleucum, the Taiwan tuber fleece flower, shows high inhibitory activity against ACC in liver microsomes with IC50 = 0.03 mg/ml. After 4 weeks of feeding, body weight and levels of blood glucose, insulin, triacylglycerol, total cholesterol, and leptin are significantly reduced in mice, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
isocitrate
-
nearly absolute requirement for tricarboxylate activators such as citrate or isocitrate
additional information
-
more than 200% increase in activity when rats were treated with troglitazone for 18 days
-
citrate
-
nearly absolute requirement for tricarboxylate activators such as citrate or isocitrate
citrate
-
completely inactive in absence of the allosteric activator citrate
citrate
-
an intermediate metabolite, activates hypothalamic ACC and is involved in the control of energy mobilization
glutamate
-
role as physiological activator postulated, 4fold activation in absence of citrate, affects phosphorylation of enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000842
(2-[(1E,3Z)-hexa-1,3,5-trien-1-yl]quinolin-4-yl)(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)methanone
Rattus norvegicus
-
ACC1
0.00891
(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)(quinolin-4-yl)methanone
Rattus norvegicus
-
ACC1
0.00301
(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)[3-(1H-pyrazol-3-yl)phenyl]methanone
Rattus norvegicus
-
ACC1
0.00127
(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)[3-(1H-pyrazol-4-yl)phenyl]methanone
Rattus norvegicus
-
ACC1
0.00162
1'-(1H-indazol-7-ylcarbonyl)-5-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000163
1'-(1H-indazol-7-ylcarbonyl)-6,7-dimethylspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00132
1'-(1H-indazol-7-ylcarbonyl)-6,8-dimethylspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000562
1'-(1H-indazol-7-ylcarbonyl)-6-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000634
1'-(1H-indazol-7-ylcarbonyl)-6-methylspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00253
1'-(1H-indazol-7-ylcarbonyl)-7-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00085
1'-(1H-indazol-7-ylcarbonyl)-7-methylspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00221
1'-(1H-indazol-7-ylcarbonyl)-7-phenylspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000303
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidine]-6-carboxylic acid
Rattus norvegicus
-
ACC1
0.000031
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1-methyl-1H-pyrazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.0000075
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1-methyl-1H-pyrazol-4-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000018
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1H-pyrazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.0000074
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(1H-pyrazol-4-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000019
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(2-methyl-1,3-oxazol-4-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000017
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(2-methyl-1,3-oxazol-5-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000018
1'-[(7-methyl-1H-indazol-5-yl)carbonyl]-6-(5-methyl-1H-pyrazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000012
1-[(3,7-dimethyl-1H-indazol-5-yl)carbonyl]-5'-(propan-2-yloxy)spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000249
1-[(3,7-dimethyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000766
1-[(3-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.00003
1-[(7-methyl-1H-indazol-5-yl)carbonyl]-5'-(propan-2-yloxy)spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.0000246
1-[(7-methyl-1H-indazol-5-yl)carbonyl]-6'-(1-methyl-1H-pyrazol-4-yl)spiro[piperidine-4,2'-pyrano[2,3-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000154
1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.00338
1H-indazol-7-yl(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)methanone
Rattus norvegicus
-
ACC1
0.000023
5'-(butan-2-yloxy)-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000061
5'-ethoxy-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000086
5'-methoxy-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000034
5'-methoxy-7'-methyl-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.0011
5-(tetradecyloxy)-2-furoyl-CoA
Rattus norvegicus
-
pH 7.5, 37°C, partially purified native enzyme
0.000019
5-methoxy-1'-([2-(1-methyl-1H-pyrazol-3-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000101
5-methoxy-1'-([2-(pyridazin-4-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000026
5-methoxy-1'-([2-(pyridin-2-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000026
5-methoxy-1'-([2-(pyridin-3-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00006
5-methoxy-1'-([2-(pyridin-4-yl)-1H-benzimidazol-5-yl]carbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000016
5-methoxy-1'-[(2-phenyl-1H-benzimidazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000104
5-methoxy-1'-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000065
5-[(5-methoxy-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)carbonyl]-1H-indole-2-carboxamide
Rattus norvegicus
-
ACC1
0.000043
5-[(5-methoxy-4-oxo-3,4-dihydro-1'H-spiro[chromene-2,4'-piperidin]-1'-yl)carbonyl]-N-methyl-1H-indole-2-carboxamide
Rattus norvegicus
-
ACC1
0.000975
6'-(1-methyl-1H-pyrazol-4-yl)-1-([2-(1-methyl-1H-pyrazol-3-yl)-1H-benzimidazol-6-yl]carbonyl)spiro[piperidine-4,2'-pyrano[2,3-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.00135
6'-amino-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000182
6'-methoxy-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[2,3-c]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000366
6'-methyl-1-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[piperidine-4,2'-pyrano[3,2-b]pyridin]-4'(3'H)-one
Rattus norvegicus
-
ACC1
0.000036
6,7-dimethyl-1'-[(3-methyl-1H-indazol-6-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000022
6,7-dimethyl-1'-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000013
6-(3,5-dimethyl-1,2-oxazol-4-yl)-1'-[(7-methyl-1H-indazol-5-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00183
6-chloro-1'-(1H-indazol-7-ylcarbonyl)-5-methoxyspiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.00139
6-chloro-1'-(1H-indazol-7-ylcarbonyl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Rattus norvegicus
-
ACC1
0.000325
anthracen-9-yl(4-[(2-methylquinolin-6-yl)methyl]piperidin-1-yl)methanone
Rattus norvegicus
-
ACC1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme ACC1; gene ACACA, encoding isozyme ACC1 or ACC-alpha
GenBank
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
37571, 37579, 37586, 37592, 37593, 37599, 37609, 37612, 665526, 671950, 693951, 702619, 705505, 714466, 715851
additional information
ACC1 and ACC2 tissue expression pattern, overview
additional information
-
ACC1 is found primarily in lipogenic tissues such as the liver and adipose tissue whereas ACC2 is the predominate form found in oxidative tissues, skeletal muscle and heart
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACACA_RAT
2345
0
265194
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10000000
-
gel filtration enzyme exists in two polymeric forms of MW 2000000 and 10000000, interconvertible by phosphorylation and dephosphorylation. The 10000000 MW form predomionantly exists in preparations of freeze-clamped liver
110000
-
x * 110000, ultracentrifugation in presence of 6 M guanidine hydrochloride and 0.1 M 2-mercaptoethanol
2000000
-
gel filtration enzyme exists in two polymeric forms of MW 2000000 and 10000000,interconvertible by phosphorylation and dephosphorylation. The 2000000 MW form predominates in preparations of unfrozen liver and is converted to the 10000000 MW form by dephosphorylation
250000
265000
272000
-
x * 272000, and a minor band at 265000 MW, hindlimb muscle, SDS-PAGE
280000
250000
-
x * 250000, SDS-PAGE, 2 polymeric forms of MW 2000000 Da, and MW 10000000 Da
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
polymer
additional information
?
-
x * 240000-260000, SDS-PAGE of enzyme dissociated in 1% SDS, 8 M urea and 5 mM DTT
?
-
x * 110000, ultracentrifugation in presence of 6 M guanidine hydrochloride and 0.1 M 2-mercaptoethanol
polymer
-
x * 250000, SDS-PAGE, 2 polymeric forms of MW 2000000 Da, and MW 10000000 Da
polymer
-
x * 240000-260000, SDS-PAGE, polymeric form shows filamentous structure
additional information
domain structure and organization of the isozyme, evolution and functional domains, overview
additional information
domain structure and organization of the isozyme, evolution and functional domains, overview
additional information
-
a large, multi-domain single polypeptide enzyme which forms complexes of several protomers, overview, polymerization is promoted by citrate, isocitrate, malonate, sulfate, and phosphate, while long-chain fatty acids promote the complex dissociation
additional information
domain structure and organization of the isozyme, evolution and functional domains, overview
additional information
domain structure and organization of the isozyme, evolution and functional domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
the enzyme in liver is regulated by reversible phosphorylation, differential phosphorylation of isozymes, overview
phosphoprotein
phosphoprotein
-
AMP-activated protein kinase phosphorylates and inactivates enzyme activity
phosphoprotein
-
AMP-activated protein kinase phosphorylates and inactivates enzyme activity in liver
phosphoprotein
-
enzyme is phosphorylated and inactivated by AMP-activated protein kinase
phosphoprotein
-
Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview
phosphoprotein
the enzyme in liver is regulated by reversible phosphorylation, differential phosphorylation of isozymes, overview
phosphoprotein
-
ACC is inactivated by phosphorylation through AMP-activated protein kinase, AMPK, citrate treatment inhibits 75% of control hypothalamic AMPK phosphorylation during fasting, overview
phosphoprotein
-
activated AMP-activated protein kinase, AMPK, phosphorylates and inhibits acetyl-CoA carboxylase, AMPK is itself regulated by reversible phosphorylation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
downregulation of the enzyme by siRNA transfected into the INS-1-derived cell line 832/13 affects insulin secretion, the enzyme activity in 832/13 cells and islets is reduced by 46-80% compared to the untreated cells, and glucose-stimulated insulin secretion is reduced by 70% in 832/13 cells and by 33% in islets, phenotypes, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, 50 mM imidazole HCl, 0.1 mM EDTA, 0.02% sodium azide, 20% glycerol, 25 mM citrate, pH 7.5, stable for up to 1 week
-
5°C, under N2, 20 mM sodium citrate, 10 mM potassium phosphate buffer, pH 7.5, 1 mM EDTA, 1 mM DTT, protein concentration greater than 2 mg/ml, stable for 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
c-Myc-5 monoclonal IgG column chromatography and Sephacryl S-300 gel filtration
-
native enzyme from liver by two steps of ammonium sulfate fractionation, and anion exchange chromatography
-
partially from liver by avidin affinity chromatography including a batch step
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, alternative splicing, overview
DNA and amino acid sequence determination and analysis, alternative splicing, overview
expressed in baculovirus-infected High Five insect cells as N-terminal His-tagged fusion proteins
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thampy, K.G.; Wakil, S.J.
Regulation of acetyl-coenzyme A carboxylase. I. Purification and properties of two forms of acetyl-coenzyme A carboxylase from rat liver
J. Biol. Chem.
263
6447-6453
1988
Rattus norvegicus
Abdel-Halim, M.N.; Yousufzai, S.Y.K.
Inhibition of acetyl-CoA carboxylase by a high molecular weight protein in rat liver
Z. Naturforsch. C
37
308-313
1982
Rattus norvegicus
Hardie, D.G.; Guy, P.S.; Cohen, P.
Acetyl-CoA carboxylase and fatty acid synthase from lactating rabbit and rat mammary gland
Methods Enzymol.
71
26-33
1981
Oryctolagus cuniculus, Rattus norvegicus
Ahmad, F.; Ahmad, P.M.
Acetyl-CoA carboxylase from rat mammary gland (including an additional step yielding fatty acid synthase)
Methods Enzymol.
71
16-26
1981
Rattus norvegicus
Tanabe, T.; Nakanishi, S.; Hashimoto, T.; Ogiwara, H.; Nikawa, J.I.; Numa, S.
Acetyl-CoA carboxylase from rat liver. EC 6.4.1.2 Acetyl-CoA:carbon-dioxide ligase (ADP-forming)
Methods Enzymol.
71
5-16
1981
Rattus norvegicus
Ahmad, F.; Ahmad, P.M.; Pieretti, L.; Watters, G.T.
Purification and subunit structure of rat mammary gland acetyl coenzyme A carboxylase
J. Biol. Chem.
253
1733-1737
1978
Rattus norvegicus
Miller, A.L.; Levy, H.R.
Acetyl-CoA carboxylase from rat mammary gland
Methods Enzymol.
35B
11-17
1975
Rattus norvegicus
Inoue, H.; Lowenstein, J.M.
Acetyl coenzyme A carboxylase from rat liver
Methods Enzymol.
35B
3-11
1975
Rattus norvegicus
Alberts, A.W.; Vagelos, P. R.
Acyl-CoA carboxylase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
37-82
1972
Bacillus cereus, Bos taurus, Corynebacterium glutamicum, Saccharomyces cerevisiae, Escherichia coli, Lactiplantibacillus plantarum, Mycobacterium avium, Mycolicibacterium phlei, Pigeon, Pseudomonas citronellolis, Rattus norvegicus, Triticum aestivum
-
Thampy, K.G.
Formation of malonyl coenzyme A in rat heart. Identification and purification of an isozyme of A carboxylase from rat heart
J. Biol. Chem.
264
17631-17634
1989
Rattus norvegicus
Sumida, K.; Kaneko, H.; Yoshitake, A.
Inhibition of animal acetyl-coenzyme A carboxylase by 2-(p-chlorophenoxy)-2-methylpropionic acid and 2-ethylhexanoic acid
Chemosphere
33
2201-2207
1996
Canis lupus familiaris, Oryctolagus cuniculus, Macaca mulatta, Mesocricetus auratus, Rattus norvegicus
Moule, S.K.; Edgell, N.J.; Borthwick, A.C.; Denton, R.M.
Coenzyme A is a potent inhibitor of acetyl-CoA carboxylase from rat epididymal fat-pads
Biochem. J.
283
35-38
1992
Rattus norvegicus
Rose-Kahn, G.; Bar-Tana, J.
Inhibition of rat liver acetyl-CoA carboxylase by beta, beta -tetramethyl-substituted hexadecanedioic acid (MEDICA 16)
Biochim. Biophys. Acta
1042
259-264
1990
Rattus norvegicus
Trumble, G.E.; Smith, M.A.; Winder, W.W.
Purification and characterization of rat skeletal muscle acetyl-CoA carboxylase
Eur. J. Biochem.
231
192-198
1995
Rattus norvegicus
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
Atkinson, L.L.; Kelly, S.E.; Russell, J.C.; Bar-Tana, J.; Lopaschuk, G.D.
MEDICA 16 inhibits hepatic acetyl-CoA carboxylase and reduces plasma triacylglycerol levels in insulin-resistant JCR: LA-cp rats
Diabetes
51
1548-1555
2002
Rattus norvegicus
Boone, A.N.; Chan, A.; Kulpa, J.E.; Brownsey, R.W.
Bimodal activation of acetyl-CoA carboxylase by glutamate
J. Biol. Chem.
275
10819-10825
2000
Rattus norvegicus
Thampy, G.K.; Haas, M.J.; Mooradian, A.D.
Troglitazone stimulates acetyl-CoA carboxylase activity through a post-translational mechanism
Life Sci.
68
699-708
2000
Rattus norvegicus
Tomas, E.; Tsao, T.S.; Saha, A.K.; Murrey, H.E.; Zhang Cc, C.; Itani, S.I.; Lodish, H.F.; Ruderman, N.B.
Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation
Proc. Natl. Acad. Sci. USA
99
16309-16313
2002
Rattus norvegicus
Barber, M.C.; Price, N.T.; Travers, M.T.
Structure and regulation of acetyl-CoA carboxylase genes of metazoa
Biochim. Biophys. Acta
1733
1-28
2005
Danio rerio, Saccharomyces cerevisiae, Caenorhabditis briggsae, Caenorhabditis elegans, Gallus gallus, Ciona intestinalis, Drosophila melanogaster, Escherichia coli, Ovis aries, Takifugu rubripes, Homo sapiens (O00763), Homo sapiens (Q13085), Rattus norvegicus (O70151), Rattus norvegicus (P11497), Mus musculus (Q5SWU9), Mus musculus (Q6JIZ0), Caenorhabditis elegans W09B6
Tong, L.
Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery
Cell. Mol. Life Sci.
62
1784-1803
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Hordeum vulgare, Mus musculus, Oryza sativa, Rattus norvegicus, Schizosaccharomyces pombe, Streptomyces coelicolor, Toxoplasma gondii
Freiberg, C.; Brunner, N.A.; Schiffer, G.; Lampe, T.; Pohlmann, J.; Brands, M.; Raabe, M.; Habich, D.; Ziegelbauer, K.
Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity
J. Biol. Chem.
279
26066-26073
2004
Bacillus subtilis, Escherichia coli, Staphylococcus aureus, Rattus norvegicus, Escherichia coli MG1655
Brownsey, R.W.; Boone, A.N.; Elliott, J.E.; Kulpa, J.E.; Lee, W.M.
Regulation of acetyl-CoA carboxylase
Biochem. Soc. Trans.
34
223-227
2006
Rattus norvegicus, Homo sapiens (Q13085)
Cheng, D.; Chu, C.H.; Chen, L.; Feder, J.N.; Mintier, G.A.; Wu, Y.; Cook, J.W.; Harpel, M.R.; Locke, G.A.; An, Y.; Tamura, J.K.
Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes
Protein Expr. Purif.
51
11-21
2007
Rattus norvegicus, Homo sapiens (O00763), Homo sapiens (Q13085), Homo sapiens
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
Ronnebaum, S.M.; Joseph, J.W.; Ilkayeva, O.; Burgess, S.C.; Lu, D.; Becker, T.C.; Sherry, A.D.; Newgard, C.B.
Chronic suppression of acetyl-CoA carboxylase 1 in beta-cells impairs insulin secretion via inhibition of glucose rather than lipid metabolism
J. Biol. Chem.
283
14248-14256
2008
Rattus norvegicus (P11497)
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
Corbett, J.W.; Freeman-Cook, K.D.; Elliott, R.; Vajdos, F.; Rajamohan, F.; Kohls, D.; Marr, E.; Zhang, H.; Tong, L.; Tu, M.; Murdande, S.; Doran, S.D.; Houser, J.A.; Song, W.; Jones, C.J.; Coffey, S.B.; Buzon, L.; Minich, M.L.; Dirico, K.J.; Tapley, S.; McPherson, R.K.; Sugarman, E.; Harwood, H.J.; Esler, W.
Discovery of small molecule isozyme non-specific inhibitors of mammalian acetyl-CoA carboxylase 1 and 2
Bioorg. Med. Chem. Lett.
20
2383-2388
2010
Homo sapiens, Rattus norvegicus
Chen, C.H.; Chang, M.Y.; Lin, Y.S.; Lin, D.G.; Chen, S.W.; Chao, P.M.
A herbal extract with acetyl-coenzyme A carboxylase inhibitory activity and its potential for treating metabolic syndrome
Metab. Clin. Exp.
58
1297-1305
2009
Homo sapiens, Mus musculus, Rattus norvegicus, Mus musculus C57/BL6J
Bengtsson, C.; Blaho, S.; Saitton, D.B.; Brickmann, K.; Broddefalk, J.; Davidsson, O.; Drmota, T.; Folmer, R.; Hallberg, K.; Hallen, S.; et al.
Design of small molecule inhibitors of acetyl-CoA carboxylase 1 and 2 showing reduction of hepatic malonyl-CoA levels in vivo in obese Zucker rats
Bioorg. Med. Chem.
19
3039-3053
2011
Homo sapiens, Rattus norvegicus
Keil, S.; Mueller, M.; Zoller, G.; Haschke, G.; Schroeter, K.; Glien, M.; Ruf, S.; Focken, I.; Herling, A.W.; Schmoll, D.
Identification and synthesis of novel inhibitors of acetyl-CoA carboxylase with in vitro and in vivo efficacy on fat oxidation
J. Med. Chem.
53
8679-8687
2010
Homo sapiens, Rattus norvegicus
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