Any feedback?
Information on EC 6.4.1.2 - acetyl-CoA carboxylase and Organism(s) Mus musculus and UniProt Accession Q5SWU9
for references in articles please use BRENDA:EC6.4.1.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
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: Mus musculus
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
ACCase
-
-
-
-
Acetyl CoA carboxylase
-
-
-
-
Acetyl coenzyme A carboxylase
-
-
-
-
Acetyl-coenzyme A carboxylase
-
-
-
-
Carboxylase, acetyl coenzyme A
-
-
-
-
additional information
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
Q6JIZ0
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
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
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
Q5SWU9, Q6JIZ0
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
Q5SWU9, Q6JIZ0
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
Q5SWU9, Q6JIZ0
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
-
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
Q5SWU9, Q6JIZ0
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
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
ACC plays an important role in energy balance by controlling malonyl-CoA synthesis
-
-
?
additional information
?
-
-
isozymes ACC1 and ACC2 play roles in lipid metabolism in adipose tissue, overview
-
-
?
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
Q5SWU9, Q6JIZ0
first committed step in fatty acid biosynthesis, hormonal, nutrient, and tissue-specific regulation of ACC genes, regulation of isozyme activity, overview
-
-
?
additional information
?
-
-
isozymes ACC1 and ACC2 play roles in lipid metabolism in adipose tissue, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
Q5SWU9, Q6JIZ0
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
-
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
-
ACC plays an important role in energy balance by controlling malonyl-CoA synthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1'-(10,11-dihydro-5H-dibenzo[b,f]azepin-5-ylcarbonyl)-6-morpholin-4-yl-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
7% inhibition at 0.01 mM
1'-(10H-phenothiazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
16% inhibition at 0.01 mM
1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
51% inhibition at 0.005 mM
1'-(anthracen-9-ylcarbonyl)-3-(morpholin-4-ylcarbonyl)-1,4'-bipiperidine
-
i.e. CP-640186 or bispiperidylcarboxamide derivative I with a tricyclic hydrophobic core, shows inhibition of both ACC1 and ACC2
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-6-morpholin-4-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-(2-oxopyrrolidin-1-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-(4-methylpiperazin-1-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-methyl-6-morpholin-4-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-morpholin-4-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-piperidin-1-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-pyrrolidin-1-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
44% inhibition at 0.01 mM
1'-[(4,8-dimethoxyquinolin-2-yl)carbonyl]-6-(1H-1,2,4-triazol-3-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
-
complete inhibition at 0.005 mM
1'-[(4,8-dimethoxyquinolin-2-yl)carbonyl]-6-[(1-methyl-1H-pyrazol-5-yl)amino]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
complete inhibition at 0.005 mM
6-(2-oxopyrrolidin-1-yl)-1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
-
6-morpholin-4-yl-1'-(10H-phenothiazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
64% inhibition at 0.01 mM
6-morpholin-4-yl-1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
-
7-(3,5-dimethylmorpholin-4-yl)-1'-[(2,6-diphenylpyridin-4-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
-
-
7-morpholin-4-yl-1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
-
-
N-(3-[1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidin]-6-yl]-1-methylprop-2-yn-1-yl)acetamide
-
-
N-[1'-(10,11-dihydro-5H-dibenzo[b,f]azepin-5-ylcarbonyl)-4-oxo-3,4-dihydro-1H-spiro[naphthalene-2,4'-piperidin]-6-yl]butanamide
-
4% inhibition at 0.01 mM
N-[1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidin]-6-yl]-N-methylbutanamide
-
83% inhibition at 0.01 mM
N-[1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidin]-6-yl]butanamide
-
-
N-[4-oxo-1'-(10H-phenothiazin-10-ylcarbonyl)-3,4-dihydro-1H-spiro[naphthalene-2,4'-piperidin]-6-yl]butanamide
-
48% inhibition at 0.01 mM
N-[4-oxo-1'-(10H-phenoxazin-10-ylcarbonyl)-3,4-dihydro-1H-spiro[naphthalene-2,4'-piperidin]-6-yl]butanamide
-
-
soraphen A
-
macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain
additional information
-
phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, FOP herbicides are weak inhibitors of the murine enzyme
-
additional information
-
synthesis of spiro[chroman-2,4-piperidin]-4-one derivatives as ACC inhibitors, overview
-
additional information
-
an ethanol extract of Polygonum hypoleucum, the Taiwan tuber fleece flower, shows high inhibitory activity against ACC. 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
additional information
-
stevioside does not influence activity in the presence of 11.1 mM glucose
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000055
1'-(anthracen-9-ylcarbonyl)-3-(morpholin-4-ylcarbonyl)-1,4'-bipiperidine
Mus musculus
-
ACC1 and ACC2
0.000006
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-6-morpholin-4-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000014
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-(2-oxopyrrolidin-1-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000027
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-(4-methylpiperazin-1-yl)spiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000002
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-methyl-6-morpholin-4-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000026
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-morpholin-4-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000036
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-piperidin-1-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000061
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-7-pyrrolidin-1-ylspiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.0012
1'-[(2,6-diphenylpyridin-4-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000236
6-(2-oxopyrrolidin-1-yl)-1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000099
6-morpholin-4-yl-1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000059
7-(3,5-dimethylmorpholin-4-yl)-1'-[(2,6-diphenylpyridin-4-yl)carbonyl]spiro[chromene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000208
7-morpholin-4-yl-1'-(10H-phenoxazin-10-ylcarbonyl)-1H-spiro[naphthalene-2,4'-piperidin]-4(3H)-one
Mus musculus
-
-
0.000061
N-(3-[1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidin]-6-yl]-1-methylprop-2-yn-1-yl)acetamide
Mus musculus
-
-
0.000006
N-[1'-[(2,6-diphenylpyridin-4-yl)carbonyl]-4-oxo-3,4-dihydrospiro[chromene-2,4'-piperidin]-6-yl]butanamide
Mus musculus
-
-
0.000101
N-[4-oxo-1'-(10H-phenoxazin-10-ylcarbonyl)-3,4-dihydro-1H-spiro[naphthalene-2,4'-piperidin]-6-yl]butanamide
Mus musculus
-
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
specific knockdown of Acc1 leads to decreased lipoylation and mitochondrial fragmentation. Simultaneous knockdown of ACSF3, encoding a mitochondrial malonyl-CoA synthetase, results in almost complete ablation of protein lipoylation
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_MOUSE
2345
0
265257
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
domain structure and organization, evolution and functional domains, overview
additional information
Q6JIZ0
domain structure and organization, 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, evolution and functional domains, overview
additional information
Q6JIZ0
domain structure and organization, evolution and functional domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
Q5SWU9, Q6JIZ0
reversible phosphorylation has regulatory function, differential phosphorylation of isozymes, overview
phosphoprotein
phosphoprotein
-
Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview
phosphoprotein
Q5SWU9, Q6JIZ0
reversible phosphorylation has regulatory function, differential phosphorylation of isozymes, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
ACC2 knockout mutant mice are protected against diet-induced obesity and diabetes and show a 80% increased palmitate oxidation level in adipocytes which remains increased in presence of insulin, also the glucose oxidation is 2fold increased in mutant mice compared to wild-type mice
additional information
-
ACC2-deficient mice show continous fatty acid oxidation and reduced body weight and body fat
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosome 12 of all genotypes contains an ACACA pseudogene named acaca-psi, alternative splicing, overview
Q5SWU9, Q6JIZ0
DNA and amino acid sequence determination and analysis, chromosome 12 of all genotypes contains an ACACA pseudogene named acaca-psi, alternative splicing, overview
Q5SWU9, Q6JIZ0
expression analysis of genes involved in energy metabolism, including gene Acc2, in wild-type and Acc2-knockout mutant mice
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
pharmacological inhibition of the ACC system is of potential use for treatment of key components of the metabolic syndrome, plasma and hepatic metabolic parameters after fasting and after the hyperinsulinaemic euglycaemic clamp, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levert, K.L.; Waldrop, G.L.; Stephens, J.M.
A biotin analog inhibits acetyl-CoA carboxylase activity and adipogenesis
J. Biol. Chem.
277
16347-16350
2002
Mus musculus
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
Oh, W.; Abu-Elheiga, L.; Kordari, P.; Gu, Z.; Shaikenov, T.; Chirala, S.S.; Wakil, S.J.
Glucose and fat metabolism in adipose tissue of acetyl-CoA carboxylase 2 knockout mice
Proc. Natl. Acad. Sci. USA
102
1384-1389
2005
Mus musculus
Chen, J.; Jeppesen, P.B.; Nordentoft, I.; Hermansen, K.
Stevioside improves pancreatic beta-cell function during glucotoxicity via regulation of acetyl-CoA carboxylase
Am. J. Physiol. Endocrinol. Metab.
292
E1906-E1916
2007
Mus musculus
Shinde, P.; Srivastava, S.K.; Odedara, R.; Tuli, D.; Munshi, S.; Patel, J.; Zambad, S.P.; Sonawane, R.; Gupta, R.C.; Chauthaiwale, V.; Dutt, C.
Synthesis of spiro[chroman-2,4-piperidin]-4-one derivatives as acetyl-CoA carboxylase inhibitors
Bioorg. Med. Chem. Lett.
19
949-953
2008
Mus musculus
Schreurs, M.; van Dijk, T.H.; Gerding, A.; Havinga, R.; Reijngoud, D.J.; Kuipers, F.
Soraphen, an inhibitor of the acetyl-CoA carboxylase system, improves peripheral insulin sensitivity in mice fed a high-fat diet
Diabetes Obes. Metab.
11
987-991
2009
Mus musculus
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
Monteuuis, G.; Suomi, F.; Keraetaer, J.M.; Masud, A.J.; Kastaniotis, A.J.
A conserved mammalian mitochondrial isoform of acetyl-CoA carboxylase ACC1 provides the malonyl-CoA essential for mitochondrial biogenesis in tandem with ACSF3
Biochem. J.
474
3783-3797
2017
Homo sapiens (Q13085), Homo sapiens, Mus musculus (Q5SWU9), Mus musculus
EXTERNAL LINKS (specific for EC-Number 6.4.1.2)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
