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Literature summary extracted from

  • Tong, L.
    Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery (2005), Cell. Mol. Life Sci., 62, 1784-1803.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.4.1.2 citrate feedforward allosteric activator Mus musculus
6.4.1.2 citrate feedforward allosteric activator Homo sapiens
6.4.1.2 citrate feedforward allosteric activator Rattus norvegicus

Application

EC Number Application Comment Organism
6.4.1.2 agriculture the enzyme is a target for development of herbicides Hordeum vulgare
6.4.1.2 agriculture the enzyme is a target for development of herbicides Arabidopsis thaliana
6.4.1.2 agriculture the enzyme is a target for development of herbicides Oryza sativa
6.4.1.2 biotechnology the enzyme is a target for development of herbicides Hordeum vulgare
6.4.1.2 biotechnology the enzyme is a target for development of herbicides Arabidopsis thaliana
6.4.1.2 biotechnology the enzyme is a target for development of herbicides Oryza sativa
6.4.1.2 drug development the enzyme is a target for drug development in case of obesity, diabetes, and other symptoms of the metabolic syndrome Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.4.1.2 regulation of acc expression, overview Escherichia coli
6.4.1.2 regulation of acc expression, overview Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.4.1.2
-
Escherichia coli
6.4.1.2 crystallization of the carboxyltranferase domain CT in complex with CoA, inhibitor CP-640186, or herbicides haloxyfop or diclofop Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
6.4.1.2 L1705I/V1967I the mutant is not more sensitive to FOP herbicides than the wild-type enzyme Saccharomyces cerevisiae
6.4.1.2 additional information ACC2-deficient mice show continous fatty acid oxidation and reduced body weight and body fat Mus musculus
6.4.1.2 additional information enzyme deletion is lethal Saccharomyces cerevisiae
6.4.1.2 additional information missense mutation of the biotin carboxylase domain located at the active site disrupts catalysis Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.4.1.2 CP-640186 inhibition of both isozymes Acc1 and Acc2, an anthracene fluorophore, probably binds to the biotin binding site Homo sapiens
6.4.1.2 CP-640186 an anthracene fluorophore, probably binds to the biotin binding site Saccharomyces cerevisiae
6.4.1.2 Diclofop
-
Arabidopsis thaliana
6.4.1.2 FOP herbicides IC50 of 0.005-0.02 mM Toxoplasma gondii
6.4.1.2 Haloxyfop
-
Arabidopsis thaliana
6.4.1.2 long-chain fatty acids potent feedback inhibition Homo sapiens
6.4.1.2 long-chain fatty acids potent feedback inhibition Mus musculus
6.4.1.2 long-chain fatty acids potent feedback inhibition Rattus norvegicus
6.4.1.2 moiramide B
-
Escherichia coli
6.4.1.2 additional information herbicide mode and site of action Arabidopsis thaliana
6.4.1.2 additional information no inhibition by soraphen A Escherichia coli
6.4.1.2 additional information phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, overview, FOP herbicides are weak inhibitors of the human enzyme Homo sapiens
6.4.1.2 additional information cereal crops are resistant to FOP herbicides, overview Hordeum vulgare
6.4.1.2 additional information phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, FOP herbicides are weak inhibitors of the murine enzyme Mus musculus
6.4.1.2 additional information cereal crops are resistant to FOÜ herbicides, overview Oryza sativa
6.4.1.2 additional information phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, FOP herbicides are weak inhibitors of the rat enzyme Rattus norvegicus
6.4.1.2 additional information FOP herbicides are weak inhibitors of the yeast enzyme Saccharomyces cerevisiae
6.4.1.2 additional information no inhibition by soraphen A Streptomyces coelicolor
6.4.1.2 additional information no inhibition by soraphen A Toxoplasma gondii
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Arabidopsis thaliana
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Homo sapiens
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Hordeum vulgare
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Mus musculus
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Oryza sativa
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Rattus norvegicus
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Saccharomyces cerevisiae
6.4.1.2 soraphen A macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain Schizosaccharomyces pombe

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4.1.2 additional information
-
additional information kinetics Escherichia coli
6.4.1.2 0.1
-
biotin isolated biotin carboxylase domain Escherichia coli
6.4.1.2 3
-
biotin isolated carboxyltransferase domain Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.4.1.2 apicoplast
-
Toxoplasma gondii 20011
-
6.4.1.2 chloroplast
-
Hordeum vulgare 9507
-
6.4.1.2 chloroplast
-
Arabidopsis thaliana 9507
-
6.4.1.2 chloroplast
-
Oryza sativa 9507
-
6.4.1.2 cytosol
-
Hordeum vulgare 5829
-
6.4.1.2 cytosol
-
Arabidopsis thaliana 5829
-
6.4.1.2 cytosol
-
Oryza sativa 5829
-
6.4.1.2 cytosol the enzyme is anchored to the outer membrane of the mitochondrion Homo sapiens 5829
-
6.4.1.2 mitochondrion
-
Hordeum vulgare 5739
-
6.4.1.2 mitochondrion
-
Oryza sativa 5739
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Mus musculus
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Escherichia coli
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Homo sapiens
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Rattus norvegicus
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Saccharomyces cerevisiae
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Hordeum vulgare
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Arabidopsis thaliana
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Schizosaccharomyces pombe
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Streptomyces coelicolor
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Oryza sativa
6.4.1.2 Mg2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Toxoplasma gondii
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Mus musculus
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Escherichia coli
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Homo sapiens
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Rattus norvegicus
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Saccharomyces cerevisiae
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Hordeum vulgare
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Arabidopsis thaliana
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Schizosaccharomyces pombe
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Streptomyces coelicolor
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Oryza sativa
6.4.1.2 Mn2+ the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis Toxoplasma gondii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.4.1.2 265000
-
1 * 265000, isozyme Acc1, 1 * 280000, isozyme Acc2 Homo sapiens
6.4.1.2 280000
-
1 * 265000, isozyme Acc1, 1 * 280000, isozyme Acc2 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.4.1.2 ATP + acetyl-CoA + HCO3- Escherichia coli
-
ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Arabidopsis thaliana
-
ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Schizosaccharomyces pombe
-
ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Toxoplasma gondii
-
ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Hordeum vulgare biological function, overview ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Oryza sativa biological function, overview ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Mus musculus 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 ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Rattus norvegicus 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 ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Streptomyces coelicolor the enzyme activity is involved in biosynthesis of fatty acids as well as polyketids, which are precursors of pharmaceutically important antibiotics, anticancer agents and other drugs ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Homo sapiens the enzyme influences the fatty acid oxidation, body weight, and body fat levels, 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, regulation of enzyme activity ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- Saccharomyces cerevisiae the enzyme is essential for viability ADP + malonyl-CoA + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.4.1.2 Arabidopsis thaliana
-
-
-
6.4.1.2 Escherichia coli
-
-
-
6.4.1.2 Homo sapiens
-
two isozymes Acc1 and Acc2
-
6.4.1.2 Hordeum vulgare
-
-
-
6.4.1.2 Mus musculus
-
two isozymes Acc1 and Acc2
-
6.4.1.2 Oryza sativa
-
-
-
6.4.1.2 Rattus norvegicus
-
two isozymes Acc1 and Acc2
-
6.4.1.2 Saccharomyces cerevisiae
-
-
-
6.4.1.2 Schizosaccharomyces pombe
-
-
-
6.4.1.2 Streptomyces coelicolor
-
-
-
6.4.1.2 Toxoplasma gondii
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.4.1.2 additional information the enzyme is biotinylated Mus musculus
6.4.1.2 additional information the enzyme is biotinylated Escherichia coli
6.4.1.2 additional information the enzyme is biotinylated Homo sapiens
6.4.1.2 additional information the enzyme is biotinylated Rattus norvegicus
6.4.1.2 additional information the enzyme is biotinylated Saccharomyces cerevisiae
6.4.1.2 additional information the enzyme is biotinylated Hordeum vulgare
6.4.1.2 additional information the enzyme is biotinylated Arabidopsis thaliana
6.4.1.2 additional information the enzyme is biotinylated Schizosaccharomyces pombe
6.4.1.2 additional information the enzyme is biotinylated Streptomyces coelicolor
6.4.1.2 additional information the enzyme is biotinylated Oryza sativa
6.4.1.2 additional information the enzyme is biotinylated Toxoplasma gondii
6.4.1.2 phosphoprotein Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview Mus musculus
6.4.1.2 phosphoprotein Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview Homo sapiens
6.4.1.2 phosphoprotein Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Mus musculus
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Escherichia coli
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Homo sapiens
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Rattus norvegicus
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Saccharomyces cerevisiae
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Hordeum vulgare
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Arabidopsis thaliana
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Schizosaccharomyces pombe
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Streptomyces coelicolor
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Oryza sativa
6.4.1.2 ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA two-step reaction mechanism, structure-activity relationship Toxoplasma gondii

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.4.1.2 adipose tissue isozyme Acc1 Mus musculus
-
6.4.1.2 adipose tissue isozyme Acc1 Homo sapiens
-
6.4.1.2 adipose tissue isozyme Acc1 Rattus norvegicus
-
6.4.1.2 brain
-
Rattus norvegicus
-
6.4.1.2 heart isozyme Acc2 Mus musculus
-
6.4.1.2 heart isozyme Acc2 Homo sapiens
-
6.4.1.2 heart isozyme Acc2 Rattus norvegicus
-
6.4.1.2 liver isozyme Acc1 Mus musculus
-
6.4.1.2 liver isozyme Acc1 Homo sapiens
-
6.4.1.2 liver isozyme Acc1 Rattus norvegicus
-
6.4.1.2 mammary gland lactating, isozyme Acc1 Mus musculus
-
6.4.1.2 mammary gland lactating, isozyme Acc1 Homo sapiens
-
6.4.1.2 mammary gland lactating, isozyme Acc1 Rattus norvegicus
-
6.4.1.2 skeletal muscle isozyme Acc2 Mus musculus
-
6.4.1.2 skeletal muscle isozyme Acc2 Homo sapiens
-
6.4.1.2 skeletal muscle isozyme Acc2 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.4.1.2 ATP + acetyl-CoA + HCO3-
-
Escherichia coli ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3-
-
Arabidopsis thaliana ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3-
-
Schizosaccharomyces pombe ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3-
-
Toxoplasma gondii ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- biological function, overview Hordeum vulgare ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- biological function, overview Oryza sativa ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- 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 Mus musculus ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- 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 Rattus norvegicus ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the enzyme activity is involved in biosynthesis of fatty acids as well as polyketids, which are precursors of pharmaceutically important antibiotics, anticancer agents and other drugs Streptomyces coelicolor ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the enzyme influences the fatty acid oxidation, body weight, and body fat levels, 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, regulation of enzyme activity Homo sapiens ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the enzyme is essential for viability Saccharomyces cerevisiae ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Mus musculus ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Homo sapiens ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Rattus norvegicus ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Saccharomyces cerevisiae ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Hordeum vulgare ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Arabidopsis thaliana ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Schizosaccharomyces pombe ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Streptomyces coelicolor ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Oryza sativa ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase Toxoplasma gondii ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + acetyl-CoA + HCO3- the two-step reaction includes two catalytic activities at two catalytic sites: the biotin carboxylase and the carboxyltransferase, regulation of enzyme activity Escherichia coli ADP + malonyl-CoA + phosphate
-
?
6.4.1.2 ATP + biotin + HCO3- free biotin can be used as carboxyl acceptor with low activity Escherichia coli ADP + ? + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
6.4.1.2 monomer 1 * 265000, isozyme Acc1, 1 * 280000, isozyme Acc2 Homo sapiens
6.4.1.2 More a large, multi-domain enzyme Hordeum vulgare
6.4.1.2 More a large, multi-domain enzyme Arabidopsis thaliana
6.4.1.2 More a large, multi-domain enzyme Schizosaccharomyces pombe
6.4.1.2 More a large, multi-domain enzyme Oryza sativa
6.4.1.2 More a large, multi-domain enzyme, domain organization, structure analysis, overview Saccharomyces cerevisiae
6.4.1.2 More 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 Homo sapiens
6.4.1.2 More 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 Mus musculus
6.4.1.2 More 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 Rattus norvegicus
6.4.1.2 More the alpha- and beta-subunits of the carboxyltransferase domain are shared with the propionyl-CoA carboxylase, EC 6.4.1.3 Streptomyces coelicolor
6.4.1.2 oligomer
-
Toxoplasma gondii
6.4.1.2 oligomer subunit organization, overview Streptomyces coelicolor
6.4.1.2 oligomer subunit organization, structure analysis, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.4.1.2 ACC
-
Mus musculus
6.4.1.2 ACC
-
Escherichia coli
6.4.1.2 ACC
-
Homo sapiens
6.4.1.2 ACC
-
Rattus norvegicus
6.4.1.2 ACC
-
Saccharomyces cerevisiae
6.4.1.2 ACC
-
Hordeum vulgare
6.4.1.2 ACC
-
Arabidopsis thaliana
6.4.1.2 ACC
-
Schizosaccharomyces pombe
6.4.1.2 ACC
-
Streptomyces coelicolor
6.4.1.2 ACC
-
Oryza sativa
6.4.1.2 ACC
-
Toxoplasma gondii
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Mus musculus
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Escherichia coli
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Homo sapiens
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Rattus norvegicus
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Saccharomyces cerevisiae
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Hordeum vulgare
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Arabidopsis thaliana
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Schizosaccharomyces pombe
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Streptomyces coelicolor
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Oryza sativa
6.4.1.2 More the enzyme belongs to the family of biotin-dependent carboxylases Toxoplasma gondii

Cofactor

EC Number Cofactor Comment Organism Structure
6.4.1.2 ATP
-
Mus musculus
6.4.1.2 ATP
-
Escherichia coli
6.4.1.2 ATP
-
Homo sapiens
6.4.1.2 ATP
-
Rattus norvegicus
6.4.1.2 ATP
-
Saccharomyces cerevisiae
6.4.1.2 ATP
-
Hordeum vulgare
6.4.1.2 ATP
-
Arabidopsis thaliana
6.4.1.2 ATP
-
Schizosaccharomyces pombe
6.4.1.2 ATP
-
Streptomyces coelicolor
6.4.1.2 ATP
-
Oryza sativa
6.4.1.2 ATP
-
Toxoplasma gondii
6.4.1.2 biotin dependent on Schizosaccharomyces pombe
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Mus musculus
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Escherichia coli
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Homo sapiens
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Rattus norvegicus
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Saccharomyces cerevisiae
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Hordeum vulgare
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Arabidopsis thaliana
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Streptomyces coelicolor
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Oryza sativa
6.4.1.2 biotin dependent on, bound by the biotin carboxyl carrier protein Toxoplasma gondii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.4.1.2 0.000005
-
moiramide B
-
Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
6.4.1.2 0.005 0.02 IC50 of 0.005-0.02 mM Toxoplasma gondii FOP herbicides