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Information on EC 6.4.1.2 - acetyl-CoA carboxylase and Organism(s) Escherichia coli and UniProt Accession P0ABD5
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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: Escherichia coli
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
ACC
-
structural organization of the ACC multienzyme into distinct biotinoyl carboxyl carrier protein, biotin carboxylase, and carboxyltransferase components
ACCase
-
-
-
-
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
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 + biotin + HCO3-
ADP + ? + phosphate
-
free biotin can be used as carboxyl acceptor with low activity
-
-
?
ATP + propionyl-CoA + HCO3-
ADP + phosphate + methylmalonyl-CoA
-
no activity
-
-
?
additional information
?
-
-
acetyl-CoA carboxylase is a multifunctional biotin-dependent enzyme that catalyzes the first committed and regulated step in fatty acid biosynthesis in bacteria via a two-step reaction. Biotin carboxylase, EC 6.3.4.14, catalyzes the first half-reaction, which is an ATP-dependent carboxylation of biotin to form carboxybiotin. The second half-reaction is catalyzed by carboxyltransferase, EC 6.4.1.2, which transfers the carboxyl group from carboxybiotin to acetyl-CoA to generate malonyl-CoA
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
-
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first committed step of fatty acid synthesis
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first step in fatty acid biosynthesis via fatty acid synthase type II, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first step in fatty acid biosynthesis, the enzyme expression is negatively autoregulated by subunit AccB
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
the enzyme exhibits malonyl-CoA carboxylase and biotin carboxylase activity
-
-
?
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, regulation of enzyme activity
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
ACC catalyzes the first committed step in the synthesis of long-chain fatty acids
-
-
?
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
additional information
?
-
-
acetyl-CoA carboxylase is a multifunctional biotin-dependent enzyme that catalyzes the first committed and regulated step in fatty acid biosynthesis in bacteria via a two-step reaction. Biotin carboxylase, EC 6.3.4.14, catalyzes the first half-reaction, which is an ATP-dependent carboxylation of biotin to form carboxybiotin. The second half-reaction is catalyzed by carboxyltransferase, EC 6.4.1.2, which transfers the carboxyl group from carboxybiotin to acetyl-CoA to generate malonyl-CoA
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first committed step of fatty acid synthesis
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first step in fatty acid biosynthesis via fatty acid synthase type II, overview
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + malonyl-CoA + phosphate
-
first step in fatty acid biosynthesis, the enzyme expression is negatively autoregulated by subunit AccB
-
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
key enzyme of fatty acid biosynthesis
-
?
ATP + acetyl-CoA + HCO3-
ADP + phosphate + malonyl-CoA
-
ACC catalyzes the first committed step in the synthesis of long-chain fatty acids
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
-
conformational change accompanies biotinylation of the biotin domain
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
additional information
-
the zinc domain in bacterial carboxyltransferase belongs to the zinc ribbon class of zinc fingers, Zn domains are commonly associated with DNA binding
Mg2+
-
the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-3-benzo[1,3]dioxol-5-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
-
IC50 for the purified recombinant subunits AccA and AccD is 4 nM, for the wild-type enzyme in crude extract 11 nM
(E)-3-biphenyl-4-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
-
IC50 for the purified recombinant subunits AccA and AccD is 37 nM, for the wild-type enzyme in crude extract 288 nM
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
-
IC50 for the purified recombinant subunits AccA and AccD is 1 nM, for the wild-type enzyme in crude extract 8 nM
Acyl carrier protein
-
acylated derivatives, acyls with chain lengths from C6:0 to C20:1 are inhibitory, 0.04 mM results in 60-70% inhibition, complete inhibition not achieved even with very high concentrations
andrimid
-
i.e. (2E,4E,6E)-octa-2,4,6-trienoic acid [(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-amide, IC50 for the purified recombinant subunits AccA and AccD is 13 nM
coenzyme A-carboxybiotin
-
coenzyme A is covalently attached to carboxybiotin, bisubstrate inhibitor
Double-stranded DNA
-
inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase by complex formation and influencing the active site structure, while substrates malonyl-CoA and biocytin inhibit DNA-carboxyltransferase complex formation, overview. DNA and heparin can also bind to the enzyme simultaneously, but the binding of either molecule has a strong synergistic effect on binding of the other, binding structure and inhibition mechanism, overview
heparin
-
the DNA mimic inhibits the reaction catalyzed by carboxyltransferase in a competitive manner with respect to both malonyl-CoA and biocytin. DNA and heparin can also bind to the enzyme simultaneously, but the binding of either molecule has a strong synergistic effect on binding of the other, binding structure and inhibition mechanism, overview
palmitoyl-acyl carrier protein
5 min, 55% inhibition, decrease of inhibition thereafter. Enzyme exhibits a significant hysteresis in presence of palmitoyl-acyl carrier protein. Allosteric inhibitor, the pantothenic acid moiety of palmitoyl-acyl carrier protein is responsible for the inhibition. Competitive with respect to acetyl-CoA
-
single-stranded DNA
-
inhibits the reaction catalyzed by carboxyltransferase in a competitive manner with respect to both malonyl-CoA and biocytin. DNA and heparin can also bind to the enzyme simultaneously, but the binding of either molecule has a strong synergistic effect on binding of the other, binding structure and inhibition mechanism, overview
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, competitive with respect to malonyl-CoA, noncompetitive to biocytin, IC50 for the purified recombinant subunits AccA and AccD is 6 nM, for the wild-type enzyme in crude extract 15 nM
additional information
-
inhibitory and antibacterial potencies of pyrrolidine dione derivatives, overview
-
additional information
-
subunit AccB is a negative autoregulator of the accBC operon, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
biotin
-
required for subunit AccB activity, biotin is not involved in regulation of operon accBC transcription
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.088
palmitoyl-acyl carrier protein
pH 7.8, temperature not specified in the publication
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000004 - 0.000011
(E)-3-benzo[1,3]dioxol-5-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
0.000037 - 0.000288
(E)-3-biphenyl-4-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
0.000001 - 0.000008
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
0.000013
andrimid
Escherichia coli
-
i.e. (2E,4E,6E)-octa-2,4,6-trienoic acid [(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-amide, IC50 for the purified recombinant subunits AccA and AccD is 13 nM
0.000006
moiramide B
Escherichia coli
-
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, competitive with respect to malonyl-CoA, noncompetitive to biocytin, IC50 for the purified recombinant su
0.000004
(E)-3-benzo[1,3]dioxol-5-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
Escherichia coli
-
IC50 for the purified recombinant subunits AccA and AccD is 4 nM
0.000011
(E)-3-benzo[1,3]dioxol-5-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
Escherichia coli
-
IC50 for the wild-type enzyme in crude extract 11 nM
0.000037
(E)-3-biphenyl-4-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
Escherichia coli
-
IC50 for the purified recombinant subunits AccA and AccD is 37 nM
0.000288
(E)-3-biphenyl-4-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
Escherichia coli
-
, for IC50 for the wild-type enzyme in crude extract 288 nM
0.000001
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
Escherichia coli
-
IC50 for the purified recombinant subunits AccA and AccD is 1 nM
0.000008
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
Escherichia coli
-
IC 50 for the wild-type enzyme in crude extract 8 nM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
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
tetramer
additional information
tetramer
-
the four subunits are encoded by genes accA, accB, accC, and accD
tetramer
-
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
additional information
-
MW of biotin carboxylase subunit of acetyl-CoA carboxylase: 16688, calculation from nucleotide sequence
additional information
-
domain structure, evolution and functional domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the enzyme is biotinylated at the biotinyl domain of subunit AccB by the biotin-[acetyl-CoA carboxylase] ligase BirA, EC 6.3.4.15
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of Escherichia coli biotinylated biotin carboxyl carrier protein (BCCP) complexed with biotin carboxylase (BC) to a resolution of 2.49 A. The protein-protein complex shows a unique quaternary structure and two distinct interfaces for each biotinylated biotin carboxyl carrier protein monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
a constructed truncation mutant of subunit AccB comprising the 68 N-terminal residues is sufficient for negative regulation of accBC operon transcription, an accA and accB null mutant strain expressing the accB gene of Rhizobium trifolii is not reduced in growth under conditions that result in highly reduced growth for the wild-type strain
additional information
-
construction and isolation of mutant a strain resistant to moiramide B derivative (E)-3-benzo[1,3]dioxol-5-yl-N-[(S)-2-[(S)-2-methyl-1-((3R,4S)-4-methyl-2,5-dioxo-pyrrolidine-3-carbonyl)-propylcarbamoyl]-1-phenyl-ethyl]-acrylamide
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
large-scale purification of of intact 156-residue biotin carboxyl carrier subunit of the acetyl-CoA carboxylase and the truncated 87000 residue COOH-terminal fragment
-
recombinant His-tagged enzyme subunits AccA and AccD from strain XL 1-Blue by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme subunits AccA and AccD in strain XL 1-Blue
-
gene dedB, i.e. accD, encoding the beta subunit of the carboxyltransferase
-
genes accA, accB, accC, and accD, operon accBC shows nonlinear response to the gene copy number so that 50 or more copies result in an only 2-3fold increase in subunits AccB and AccC, AccB is a negative regulator for transcription of the accBC operon
-
overexpression of a biotin-domain peptide from the biotin carboxy carrier protein of acetyl-CoA carboxylase
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, S.J.; Cronan, J.E.
The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
J. Biol. Chem.
267
855-863
1992
Escherichia coli
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
-
Brownsey, R.W.; Zhande, R.; Boone, A.N.
Isoforms of acetyl-CoA carboxylase: structures, regulatory properties and metabolic functions
Biochem. Soc. Trans.
25
1232-1238
1997
Anabaena sp., Metazoa, Cyclotella cryptica, Escherichia coli, Homo sapiens, Mammalia, Pseudomonas sp.
Nenortas, E.; Beckett, D.
Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
J. Biol. Chem.
271
7559-7567
1996
Escherichia coli
Chapman-Smith, A.; Forbes, B.E.; Wallace, J.C.; Cronan, J.E.
Covalent modification of an exposed surface turn alters the global conformation of the biotin carrier domain of Escherichia coli acetyl-CoA carboxylase
J. Biol. Chem.
272
26017-26022
1997
Escherichia coli
Chapman-Smith, A.; Turner, D.L.; Cronan, J.E.; Morris, T.W.; Wallace, J.C.
Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase
Biochem. J.
302
881-887
1994
Escherichia coli
Davis, M.S.; Cronan, J.E., Jr.
Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein
J. Bacteriol.
183
1499-1503
2001
Escherichia coli
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
Sasaki, Y.; Nagano, Y.
Plant acetyl-CoA carboxylase: structure, biosynthesis, regulation, and gene manipulation for plant breeding
Biosci. Biotechnol. Biochem.
68
1175-1184
2004
Arabidopsis thaliana, Brassica napus, Escherichia coli, Nicotiana tabacum, Oryza sativa, Pisum sativum, Triticum aestivum
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
James, E.S.; Cronan, J.E.
Expression of two Escherichia coli acetyl-CoA carboxylase subunits is autoregulated
J. Biol. Chem.
279
2520-2527
2004
Escherichia coli
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
Bilder, P.; Lightle, S.; Bainbridge, G.; Ohren, J.; Finzel, B.; Sun, F.; Holley, S.; Al-Kassim, L.; Spessard, C.; Melnick, M.; Newcomer, M.; Waldrop, G.L.
The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme
Biochemistry
45
1712-1722
2006
Escherichia coli, Staphylococcus aureus
Benson, B.K.; Meades, G.J.; Grove, A.; Waldrop, G.L.
DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: implications for active site communication
Protein Sci.
17
34-42
2008
Escherichia coli
Broussard, T.C.; Kobe, M.J.; Pakhomova, S.; Neau, D.B.; Price, A.E.; Champion, T.S.; Waldrop, G.L.
The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase
Structure
21
650-657
2013
Escherichia coli (P0ABD8), Escherichia coli
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