6.4.1.2: acetyl-CoA carboxylase
This is an abbreviated version!
For detailed information about acetyl-CoA carboxylase, go to the full flat file.
Word Map on EC 6.4.1.2
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6.4.1.2
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amp-activated
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triglyceride
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lipogenesis
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adipose
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lipogenic
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sterol
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peroxisome
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cholesterol
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obesity
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carnitine
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malonyl-coa
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proliferator-activated
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high-fat
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adipocytes
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lipoprotein
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element-binding
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biotin
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steatosis
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lipase
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obese
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herbicide
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srebp-1c
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triacylglycerols
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diet-induced
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stearoyl-coa
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malic
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adiponectin
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nafld
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lipolysis
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monophosphate-activated
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hfd-induced
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protein-1c
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weed
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carboxylases
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aicar
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atp-citrate
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malonyl
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desaturase-1
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anti-obesity
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biotin-dependent
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hormone-sensitive
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chrebp
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5'-amp-activated
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palmitoyltransferase-1
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target-site
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adenoid
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srebf1
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anti-adipogenic
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lolium
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biotechnology
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medicine
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herbicide-resistant
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pharmacology
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synthesis
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drug development
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biofuel production
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agriculture
- 6.4.1.2
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amp-activated
- triglyceride
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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
Reaction
Synonyms
ACACA, ACACB, ACC, ACC-1, ACC-2, ACC1, Acc1a, Acc1b, Acc1p, ACC2, AccA, ACCalpha, ACCase, ACCase 1, ACCB, AccC, Acetyl CoA carboxylase, Acetyl coenzyme A carboxylase, acetyl coenzyme A carboxylase alpha, acetyl-CoA carboxylase, acetyl-CoA carboxylase 1, acetyl-CoA carboxylase 2, acetyl-CoA carboxylase A, acetyl-CoA carboxylase alpha, acetyl-CoA carboxylase B, acetyl-CoA carboxylase-2, acetyl-CoA carboxylase-alpha, acetyl-CoA-carboxylase, acetyl-CoA/propionyl-CoA carboxylase, Acetyl-coenzyme A carboxylase, acetyl-coenzyme-A carboxylase, acetylCoA carboxylase, acyl coenzyme A carboxylase, acyl-CoA carboxylase, BCCP1, BCCP2, CAC1A, CAC1B, Carboxylase, acetyl coenzyme A, Hfa1p, More, PccB
ECTree
6.4.1.2 acetyl-CoA carboxylaseAdvanced search results
results (
results (Subunits
Subunits on EC 6.4.1.2 - acetyl-CoA carboxylase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
heteromer
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the enzyme is composed of four subunits: biotin carboxyl carrier protein, biotin carboxylase, alpha-carboxyltransferase, and beta-carboxyltransferase
monomer
multimer
oligomer
polymer
tetramer
additional information
?
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multisubunit complex consisting of a 1. biotin carboxylase subunit, 2. a biotin-carboxyl carrier protein, 3. carboxyltransferase alpha- and beta-subunits
?
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plastid-localized enzyme, 4 different types of subunits: 1. biotin carboxyl carrier subunit, 2. biotin carboxylase subunit, 3. alpha-subunit of carboxyltransferase, 4. beta-subunit of carboxyltransferase
?
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4 component polypeptides: 1. Biotin carrier protein, MW 170000, 2. biotin carboxylase, which assembles as a dimer of two 49000 MW subunits, 3. and 4. the alpha-subunit and beta-subunit of carboxyl transferase, which assemble as a 130000 MW alpha2beta2 tetramer
?
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x * 265000-280000, exist minimally as dimers under non-denaturing conditions. When activated by dicarboxylic acids and tricarboxylic acids, which induce aggregation into elongated polymers it consists of 5-20 dimers. Two major form of animal acety-CoA carboxylase: ACC1 is the 265000 MW ACC-alpha-isoform, ACC-2 is the 275000-280000 MW ACC-beta-isoform
?
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x * 12000 + x * 47000 + x * 57000 + x * 72000, SDS-PAGE + 1% mercaptoethanol
?
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x * 240000-260000, SDS-PAGE of enzyme dissociated in 1% SDS, 8 M urea and 5 mM DTT
?
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x * 110000, ultracentrifugation in presence of 6 M guanidine hydrochloride and 0.1 M 2-mercaptoethanol
dimer
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2 * 230000, nonidentical, SDS-PAGE. The enzyme exists as a protomer of 480000 MW and as polymeric filaments
dimer
wild-type enzyme, and L1705I and V1967I mutant enzymes, light scattering
multimer
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most likely (alpha,beta,gamma)4 composition, two large subunits of 57000 Da: biotin carboxylase (alpha subunit) and carboxyl transferase (gamma subunit), 18600 Da biotin carrier protein (beta subunit)
multimer
Chloroflexus aurantiacus OK-70-fl / DSM 636
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most likely (alpha,beta,gamma)4 composition, two large subunits of 57000 Da: biotin carboxylase (alpha subunit) and carboxyl transferase (gamma subunit), 18600 Da biotin carrier protein (beta subunit)
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multimer
most likely (alpha,beta,gamma)4 composition, two large subunits of 57000 Da: biotin carboxylase (alpha subunit) and carboxyl transferase (gamma subunit), 18600 Da biotin carrier protein (beta subunit)
multimer
Metallosphaera sedula TH2 / ATCC 51363 / DSM 5348
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most likely (alpha,beta,gamma)4 composition, two large subunits of 57000 Da: biotin carboxylase (alpha subunit) and carboxyl transferase (gamma subunit), 18600 Da biotin carrier protein (beta subunit)
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multimer
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most likely (alpha,beta,gamma)4 composition, two large subunits of 57000 Da: biotin carboxylase (alpha subunit) and carboxyl transferase (gamma subunit), 18600 Da biotin carrier protein (beta subunit)
polymer
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x * 250000, SDS-PAGE, 2 polymeric forms of MW 2000000 Da, and MW 10000000 Da
polymer
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x * 240000-260000, SDS-PAGE, polymeric form shows filamentous structure
tetramer
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heterotetrameric plastidic enzyme form, the heterotetramer is composed of the subunits biotin carboxyl carrier protein BCCP, biotin carboxylase BC, and alpha and beta subunits of the carboxyltransferase CT
tetramer
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heterotetrameric plastidic enzyme form, the heterotetramer is composed of the subunits biotin carboxyl carrier protein BCCP, biotin carboxylase BC, and alpha and beta subunits of the carboxyltransferase CT
tetramer
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the four subunits are encoded by genes accA, accB, accC, and accD
tetramer
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the heterotetramer is composed of the subunits biotin carboxyl carrier protein BCCP of 17 kDa, biotin carboxylase BC of 49 kDa, and alpha and beta subunits of the carboxyltransferase CT of 35 kDa and 33 kDa
tetramer
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heterotetrameric plastidic enzyme form, the heterotetramer is composed of the subunits biotin carboxyl carrier protein BCCP, biotin carboxylase BC, and alpha and beta subunits of the carboxyltransferase CT
tetramer
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heterotetrameric plastidic enzyme form, the heterotetramer is composed of the subunits biotin carboxyl carrier protein BCCP of 21 kDa, biotin carboxylase BC of 53 kDa, and alpha and beta subunits of the carboxyltransferase CT of 91 kDa and 67 kDa
additional information
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plants possess a homomeric single polypeptide enzyme form in the cytosol, and a heterotetrameric plastidic enzyme form
additional information
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plants possess a homomeric single polypeptide enzyme form in the cytosol, and a heterotetrameric plastidic enzyme form
additional information
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MW of biotin carboxylase subunit of acetyl-CoA carboxylase: 16688, calculation from nucleotide sequence
additional information
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domain structure, evolution and functional domains, overview
additional information
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multisubunit enzyme consisting of biotin carboxylase, biotin carboxyl carrier protein and the alpha and beta subunits of carboxyltransferase, protein dissociates into two complexes in presence of 0.5 M KCl, when subunit complexes of biotin carboxylase and biotin carboxyl carrier protein and alpha and beta subunits of carboxyltransferase are expressed separately the activity of full size protein can be achieved by mixing the enzyme subunit complexes
additional information
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a large, multi-domain single polypeptide enzyme which forms complexes of several protomers, domain organization, 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
domain structure and organization, evolution and functional domains, overview
additional information
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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
additional information
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plants possess a homomeric single polypeptide enzyme form in the cytosol, and a heterotetrameric plastidic enzyme form
additional information
-
multisubunit enzyme consisting of biotin carboxylase, biotin carboxyl carrier protein and the alpha and beta subunits of carboxyltransferase
additional information
-
plants possess a homomeric single polypeptide enzyme form in the cytosol, and a heterotetrameric plastidic enzyme form
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
additional information
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a large, multi-domain enzyme, domain organization, structure analysis, overview
additional information
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domain structure, evolution and functional domains, overview
additional information
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domain structure determination of beta-subunit encoded by accD, the enzyme contains five motifs at the C-terminus but none at the N-terminus, overview
additional information
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the alpha- and beta-subunits of the carboxyltransferase domain are shared with the propionyl-CoA carboxylase, EC 6.4.1.3
additional information
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the core catalytic beta-subunit is a homohexameric complex of 360 kDa, structure overview, the dimeric interaction is crucial for enzyme catalysis, stability, and substrate specificity, interaction between alpha- and beta-subunits, overview
