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Information on EC 6.4.1.2 - acetyl-CoA carboxylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q00955
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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: Saccharomyces cerevisiae
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
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
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
catalytic regions analysis
-
ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA
molecular surface of the active site of the carboxyltransferase domain
-
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
-
-
-
r
ATP + acetyl-CoA + hydrogencarbonate
ADP + phosphate + malonyl-CoA
-
-
-
-
?
ATP + propionyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
enzymes Hfa1p and Acc1p are involved in mitochondrial and cytoplasmic fatty acid synthesis, respectively, Hfa1p is responsible for production of malonyl-CoA for intraorganellar fatty acid and lipoic acid synthesis
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
the enzyme is essential for viability
-
-
?
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
-
?
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 + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
enzymes Hfa1p and Acc1p are involved in mitochondrial and cytoplasmic fatty acid synthesis, respectively, Hfa1p is responsible for production of malonyl-CoA for intraorganellar fatty acid and lipoic acid synthesis
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
the enzyme is essential for viability
-
-
?
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
Diclofop
herbicide, molecular inhibition mechanism, active site binding structure involving Tyr1738 and Phe1956, binding induces large conformational changes in the enzyme
tepraloxydim
a herbicide, binding mode and structure-activity relationship, molecular inhibition mechanism, overview
soraphen A
-
macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain
additional information
-
FOP herbicides are weak inhibitors of the yeast enzyme
-
Haloxyfop
herbicide, molecular inhibition mechanism, active site binding structure involving Tyr1738 and Phe1956, binding induces large conformational changes in the enzyme
soraphen A
natural macrocyclic polyketid, inhibition mechanism, the inhibitor binds to an allosteric site in vicinity to the active site at the biotin carboxylase domain dimer interface causing only small coformational changes, binding structure and specificity
soraphen A
inhibits the enzyme allosterically by stabilizing a catalytically inactive conformation of the biotin carboxylase domain
CP-640186
-
an anthracene fluorophore, probably binds to the biotin binding site
CP-640186
-
herbicide, IC50 is 0.008 mM, noncompetititve to malonyl-CoA, molecular inhibitory mechanism, binding structure involving Leu1705 and Val1967, binds to the biotin binding site
Haloxyfop
-
herbicide, binding structure and inhibition mechanism, binds to an allosteric site
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.053
ATP
wild-type, pH 7.5, temperature not specified in the publication
0.074
ATP
mutant Y83A, pH 7.5, temperature not specified in the publication
0.11
ATP
mutant Q608R, pH 7.5, temperature not specified in the publication
0.15
ATP
mutant R656E, pH 7.5, temperature not specified in the publication
additional information
additional information
kinetics of recombinant wild-type and mutant enzymes
-
additional information
additional information
-
kinetics of recombinant wild-type and mutant enzymes
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
ATP
mutant Y83A, pH 7.5, temperature not specified in the publication
5
ATP
mutant R656E, pH 7.5, temperature not specified in the publication
8.5
ATP
wild-type, pH 7.5, temperature not specified in the publication
16
ATP
mutant Q608R, pH 7.5, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
CP-640186
Saccharomyces cerevisiae
-
herbicide, IC50 is 0.008 mM, noncompetititve to malonyl-CoA, molecular inhibitory mechanism, binding structure involving Leu1705 and Val1967, binds to the biotin binding site
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Hfa1p is a mitochondrion-specific enzyme and contains a canonical mitochondrial targeting sequence with a matrix protease cleavage site
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
reducing ACC1 expression results in globally increased histone acetylation and altered transcriptional regulation
physiological function
-
Acc1p activity regulates the availability of acetyl-CoA for histone acetyltransferases and provide an additional link between intermediary metabolism and histone acetylation and transcriptional regulation
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
wild-type enzyme, and L1705I and V1967I mutant enzymes, light scattering
additional information
additional information
-
a large, multi-domain enzyme, domain organization, structure analysis, overview
additional information
-
domain structure, evolution and functional domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of humanized mutant of yeast CT (yCT-H9) in complex with a human ACC2-selective small molecule inhibitor is determined
enzyme CT domain in complex with inhibitor tepraloxydim, hanging drop vapour diffusion method, at 4°C, 10 mg/ml protein in solution containing 0.1 M sodium citrate, pH 7.5, 8% w/v PEG 8000, 10% v/v glycerol, 5 mM tepraloxydim, and 5% v/v dimethyl sulfoxide, is mixed with reservoir solution containing 0.1 M sodium citrate, pH 5.5,8% w/v PEG 8000, and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified selenomethionyl biotin carboxylase domain free and with bound inhibitor soraphen A, sitting drop vapour diffusion method for crystallization of free enzyme: 4°C, the reservoir solution contains 0.1 M Bis-Tris propane, pH 6.0, 23% w/v PEG 3350, 0.2 M NaCl, 0.4 M MgCl2, and 5% glycerol, 12-18 days, followed by microseeding, which is essential, sitting drop vapour diffusion method for crystallization of inhibitor-bound enzyme: 50 mg/ml protein are incubated with 0.88 mM soraphen A at 4°C for 1 h prior to crystallization, the reservoir solution for crystallization at 22°C contains 0.1 M Bis-Tris, pH 5.8, 26% w/v PEG 3350, 0.1 M NaCl, 0.2 M MgCl2, 8% glycerol, and 2 mM DTT, as for the free enzyme microseeding is essential, X-ray diffraction structure determination and analysis at 1.8-2.9 A resolution, selenomethionyl multiwavelength anomalous diffraction method
purified wild-type enzyme and mutant enzymes, free or in complex with inhibitors haloxyfop or diclofop, 10 mg/ml protein with reservoir solution containing 0.1 M sodium citrate, pH 5.5, 0.2 M NaCl, 8% w/v PEG 8000, and 10% v/v glycerol, complexing by soaking of crystals in 5 mM inhibitor solution, cryoprotection by 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.5-2.8 A resolution
structure of the full-length, 500 kD holoenzyme dimer. The central region contains five domains and is important for positioning the biotin carboxylase and carboxyltransferase domains for catalysis. The structure reveals a dimer of the biotin carboxylase domain
structure of the non-catalytic central domain, to 3.0 A resolution. Structure shows a four-domain organization. A regulatory loop, which is phosphorylated at the key functional phosphorylation site, wedges into a crevice between two domains of the central domain. Large-scale conformational changes are required for substrate turnover. comparison with structure of human enzyme
crystallization of the carboxyltranferase domain CT in complex with CoA, inhibitor CP-640186, or herbicides haloxyfop or diclofop
-
purified recombinant carboxyltransferase domain comprising residues 1476-2233 in complex with CP-640186, hanging drop vapour diffusion method, crystallization of the free enzyme in a 10 mg/ml solution using a reservoir solution containing 0.1 M sodium citrate, pH 5.5, 0.2 M NaCl, 8% w/v PEG 8000, and 10% v/v glycerol, soaking of the crystals in 1 mM inhibitor CP-640186, X-ray diffraction structure determination and analyis at 2.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K73E
mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity
L1705I
site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme
L1705I/V1967I
site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme
P1760S/I1762L/M1765V/E1919Q/P1920A/H1925F/Q2028E/M2030T/G2032E
humanized mutant of yeast CT domain is generated by replacing nine active site residues of yeast CT domain with corresponding human ACC2 CT domain residues. This humanized yeast CT domain (yCT-H9) exhibits an inhibitor sensitivity profile similar to that of human ACC while maintaining high recombinant expression yields and robust crystallizability
R76E
mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity
V1967I
site-directed mutagenesis, the mutant enzyme shows 100fold decreased activity and 10fold increased Km for malonyl-CoA, but unaltered Ki for haloxyfop compared to the wild-type enzyme
W487A
mutation in the biotin carboxylase domain dimer interface, loss of catalytic activity
L1705I/V1967I
-
the mutant is not more sensitive to FOP herbicides than the wild-type enzyme
S1157A
-
mutation in potential site of phosphorylation, results in 9fold higher specific activity following glucose depletion
additional information
additional information
deletion of the alpha-helical hairpin (alpha8-alpha9, residues 940-972) in domain AC1 or the beta4A-beta4B loop in the C domain of carboxyltransferase (residues 1902-1916) abolishes the catalytic activity
additional information
-
deletion of the alpha-helical hairpin (alpha8-alpha9, residues 940-972) in domain AC1 or the beta4A-beta4B loop in the C domain of carboxyltransferase (residues 1902-1916) abolishes the catalytic activity
additional information
-
mutants of genes HFA1 and ACC1 shows different phenotypes and the enzymes cannot complement each other, the mitochondrial enzyme Hfa1p disruption mutant strain shows about 90% reduced lipoic acid concentration and does not grow on lactate or glycerol, complementation of hfa1 null mutants require full length HFA1 DNA including the mitochondrial targeting sequence, without the sequence the cDNA encoding the mitochondrial enzyme can complement the cytoplasmic acc1-defective mutant, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
rapid inactivation above. Dissociation of the tetrameric native enzyme in a mixture of monomers, dimers and trimers
37583
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low ionic strength and alkaline pH favor the rapid inactivation of the enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.3 M potassium phosphate, 50% glycerol, pH 6.5, stable for at least 1 year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged biotin carboxylase domain from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression of the CT domain comprising residues 1476-2233
humanized mutant of yeast CT domain is expressed in Escherichia coli
overexpression of the His-tagged biotin carboxylase domain in Escherichia coli strain BL21(DE3) and as selenomethionyl enzyme in strain B834(DE3)
gene hfa1, expression analysis, complementation of an acc1-defective mutant yeast strain
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
-
Saccharomyces cerevisiae is engineered to produce fatty acid-derived biofuels and chemicals from simple sugars. All three primary genes involved in fatty acid biosynthesis, namely ACC1, FAS1 and FAS2 are overexpressed. Combining this metabolic engineering strategy with terminal converting enzymes (diacylglycerol-acyltransferase,fatty acyl-CoA thioesterase,fatty acyl-CoA reductase, and wax ester synthase for TAG,fatty acid, fatty alcohol and FAEE production, respectively) improves the production levels of all biofuel molecules and chemicals, Saccharomyces cerevisiae provides a compelling platform for a scalable, controllable and economic route to biofuel molecules and chemicals
drug development
-
the structure of the enzyme's active site can be used for drug discovery
synthesis
-
in yeast engineered to produce the polyketide 6-methylsalisylic acid (6-MSA), both 6-MSA and native fatty acid levels increase by 3fold in presence of mutant S1157A which is not deactivated when glucose is depleted
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sumper, M.
Acetyl-CoA carboxylase from yeast
Methods Enzymol.
71
34-37
1981
Saccharomyces cerevisiae
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
-
Lill, U.; Kollmann-Koch, A.; Bibinger, A.; Eggerer, H.
Inhibitors of metabolic reactions. Scope and limitation of acyl-CoA-analogue CoA-thioethers
Eur. J. Biochem.
198
767-773
1991
Saccharomyces cerevisiae, Gallus gallus
Al-Feel, W.; Chirala, S.S.; Wakil, S.J.
Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase
Proc. Natl. Acad. Sci. USA
89
4538-4538
1992
Saccharomyces cerevisiae
-
Zhang, H.; Yang, Z.; Shen, Y.; Tong, L.
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase
Science
299
2064-2067
2003
Saccharomyces cerevisiae
Shen, Y.; Volrath, S.L.; Weatherly, S.C.; Elich, T.D.; Tong, L.
A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product
Mol. Cell
16
881-891
2004
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
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
Hoja, U.; Marthol, S.; Hofmann, J.; Stegner, S.; Schulz, R.; Meier, S.; Greiner, E.; Schweizer, E.
HFA1 encoding an organelle-specific acetyl-CoA carboxylase controls mitochondrial fatty acid synthesis in Saccharomyces cerevisiae
J. Biol. Chem.
279
21779-21786
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180-1A
Zhang, H.; Tweel, B.; Tong, L.
Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop
Proc. Natl. Acad. Sci. USA
101
5910-5915
2004
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
Zhang, H.; Tweel, B.; Li, J.; Tong, L.
Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with CP-640186
Structure
12
1683-1691
2004
Saccharomyces cerevisiae, Homo sapiens
Xiang, S.; Callaghan, M.M.; Watson, K.G.; Tong, L.
A different mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by tepraloxydim
Proc. Natl. Acad. Sci. USA
106
20723-20727
2009
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
Rajamohan, F.; Marr, E.; Reyes, A.R.; Landro, J.A.; Anderson, M.D.; Corbett, J.W.; Dirico, K.J.; Harwood, J.H.; Tu, M.; Vajdos, F.F.
Structure-guided inhibitor design for human acetyl-coenzyme A carboxylase by interspecies active site conversion
J. Biol. Chem.
286
41510-41519
2011
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
Galdieri, L.; Vancura, A.
Acetyl-CoA carboxylase regulates global histone acetylation
J. Biol. Chem.
287
23865-23876
2012
Saccharomyces cerevisiae
Choi, J.W.; Da Silva, N.A.
Improving polyketide and fatty acid synthesis by engineering of the yeast acetyl-CoA carboxylase
J. Biotechnol.
187
56-59
2014
Saccharomyces cerevisiae
Hunkeler, M.; Stuttfeld, E.; Hagmann, A.; Imseng, S.; Maier, T.
The dynamic organization of fungal acetyl-CoA carboxylase
Nat. Commun.
7
11196
2016
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
Wei, J.; Tong, L.
Crystal structure of the 500-kDa yeast acetyl-CoA carboxylase holoenzyme dimer
Nature
526
723-727
2015
Saccharomyces cerevisiae (Q00955), Saccharomyces cerevisiae
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