Any feedback?
Literature summary for 6.4.1.2 extracted from
- Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery (2005), Cell. Mol. Life Sci., 62, 1784-1803.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| citrate | feedforward allosteric activator | Mus musculus |  |
| citrate | feedforward allosteric activator | Homo sapiens | |
| citrate | feedforward allosteric activator | Rattus norvegicus | |
Application
| Application | Comment | Organism |
|---|---|---|
| agriculture | the enzyme is a target for development of herbicides | Hordeum vulgare |
| agriculture | the enzyme is a target for development of herbicides | Arabidopsis thaliana |
| agriculture | the enzyme is a target for development of herbicides | Oryza sativa |
| biotechnology | the enzyme is a target for development of herbicides | Hordeum vulgare |
| biotechnology | the enzyme is a target for development of herbicides | Arabidopsis thaliana |
| biotechnology | the enzyme is a target for development of herbicides | Oryza sativa |
| 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)
| Cloned (Comment) | Organism |
|---|---|
| regulation of acc expression, overview | Escherichia coli |
| regulation of acc expression, overview | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
- |
Escherichia coli |
| crystallization of the carboxyltranferase domain CT in complex with CoA, inhibitor CP-640186, or herbicides haloxyfop or diclofop | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| L1705I/V1967I | the mutant is not more sensitive to FOP herbicides than the wild-type enzyme | Saccharomyces cerevisiae |
| additional information | ACC2-deficient mice show continous fatty acid oxidation and reduced body weight and body fat | Mus musculus |
| additional information | enzyme deletion is lethal | Saccharomyces cerevisiae |
| additional information | missense mutation of the biotin carboxylase domain located at the active site disrupts catalysis | Arabidopsis thaliana |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| CP-640186 | inhibition of both isozymes Acc1 and Acc2, an anthracene fluorophore, probably binds to the biotin binding site | Homo sapiens | |
| CP-640186 | an anthracene fluorophore, probably binds to the biotin binding site | Saccharomyces cerevisiae | |
| Diclofop | - |
Arabidopsis thaliana | |
| FOP herbicides | IC50 of 0.005-0.02 mM | Toxoplasma gondii | |
| Haloxyfop | - |
Arabidopsis thaliana | |
| long-chain fatty acids | potent feedback inhibition | Homo sapiens | |
| long-chain fatty acids | potent feedback inhibition | Mus musculus | |
| long-chain fatty acids | potent feedback inhibition | Rattus norvegicus | |
| moiramide B | - |
Escherichia coli | |
| additional information | herbicide mode and site of action | Arabidopsis thaliana | |
| additional information | no inhibition by soraphen A | Escherichia coli | |
| 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 | |
| additional information | cereal crops are resistant to FOP herbicides, overview | Hordeum vulgare | |
| additional information | phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, FOP herbicides are weak inhibitors of the murine enzyme | Mus musculus | |
| additional information | cereal crops are resistant to FOÜ herbicides, overview | Oryza sativa | |
| additional information | phosphorylation inhibits isozymes Acc1 and Acc2, natural inhibitors and physiological effects, FOP herbicides are weak inhibitors of the rat enzyme | Rattus norvegicus | |
| additional information | FOP herbicides are weak inhibitors of the yeast enzyme | Saccharomyces cerevisiae | |
| additional information | no inhibition by soraphen A | Streptomyces coelicolor | |
| additional information | no inhibition by soraphen A | Toxoplasma gondii | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Arabidopsis thaliana | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Homo sapiens | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Hordeum vulgare | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Mus musculus | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Oryza sativa | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Rattus norvegicus | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Saccharomyces cerevisiae | |
| soraphen A | macrocyclic polyketide secreted by soil-dwelling myxobacterium Sorangium cellulosum, acts on the biotin carboxylase domain | Schizosaccharomyces pombe | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics | Escherichia coli | |
| 0.1 | - |
biotin | isolated biotin carboxylase domain | Escherichia coli | |
| 3 | - |
biotin | isolated carboxyltransferase domain | Escherichia coli | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| apicoplast | - |
Toxoplasma gondii | 20011 | - |
| chloroplast | - |
Hordeum vulgare | 9507 | - |
| chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| chloroplast | - |
Oryza sativa | 9507 | - |
| cytosol | - |
Hordeum vulgare | 5829 | - |
| cytosol | - |
Arabidopsis thaliana | 5829 | - |
| cytosol | - |
Oryza sativa | 5829 | - |
| cytosol | the enzyme is anchored to the outer membrane of the mitochondrion | Homo sapiens | 5829 | - |
| mitochondrion | - |
Hordeum vulgare | 5739 | - |
| mitochondrion | - |
Oryza sativa | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Mus musculus | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Escherichia coli | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Homo sapiens | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Rattus norvegicus | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Saccharomyces cerevisiae | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Hordeum vulgare | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Arabidopsis thaliana | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Schizosaccharomyces pombe | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Streptomyces coelicolor | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Oryza sativa | |
| Mg2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Toxoplasma gondii | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Mus musculus | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Escherichia coli | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Homo sapiens | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Rattus norvegicus | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Saccharomyces cerevisiae | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Hordeum vulgare | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Arabidopsis thaliana | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Schizosaccharomyces pombe | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Streptomyces coelicolor | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Oryza sativa | |
| Mn2+ | the enzyme requires Mg2+ or Mn2+ for coordinating the ATP phosphates for catalysis | Toxoplasma gondii | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 265000 | - |
1 * 265000, isozyme Acc1, 1 * 280000, isozyme Acc2 | Homo sapiens |
| 280000 | - |
1 * 265000, isozyme Acc1, 1 * 280000, isozyme Acc2 | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + acetyl-CoA + HCO3- | Escherichia coli | - |
ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | Arabidopsis thaliana | - |
ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | Schizosaccharomyces pombe | - |
ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | Toxoplasma gondii | - |
ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | Hordeum vulgare | biological function, overview | ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | Oryza sativa | biological function, overview | ADP + malonyl-CoA + phosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| ATP + acetyl-CoA + HCO3- | Saccharomyces cerevisiae | the enzyme is essential for viability | ADP + malonyl-CoA + phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Escherichia coli | - |
- |
- |
| Homo sapiens | - |
two isozymes Acc1 and Acc2 | - |
| Hordeum vulgare | - |
- |
- |
| Mus musculus | - |
two isozymes Acc1 and Acc2 | - |
| Oryza sativa | - |
- |
- |
| Rattus norvegicus | - |
two isozymes Acc1 and Acc2 | - |
| Saccharomyces cerevisiae | - |
- |
- |
| Schizosaccharomyces pombe | - |
- |
- |
| Streptomyces coelicolor | - |
- |
- |
| Toxoplasma gondii | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | the enzyme is biotinylated | Mus musculus |
| additional information | the enzyme is biotinylated | Escherichia coli |
| additional information | the enzyme is biotinylated | Homo sapiens |
| additional information | the enzyme is biotinylated | Rattus norvegicus |
| additional information | the enzyme is biotinylated | Saccharomyces cerevisiae |
| additional information | the enzyme is biotinylated | Hordeum vulgare |
| additional information | the enzyme is biotinylated | Arabidopsis thaliana |
| additional information | the enzyme is biotinylated | Schizosaccharomyces pombe |
| additional information | the enzyme is biotinylated | Streptomyces coelicolor |
| additional information | the enzyme is biotinylated | Oryza sativa |
| additional information | the enzyme is biotinylated | Toxoplasma gondii |
| phosphoprotein | Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview | Mus musculus |
| phosphoprotein | Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview | Homo sapiens |
| phosphoprotein | Acc1 and Acc2 can be phosphorylated by protein kinase A and cAMP depndent protein kinase, overview | Rattus norvegicus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Mus musculus | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Escherichia coli | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Homo sapiens | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Rattus norvegicus | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Saccharomyces cerevisiae | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Hordeum vulgare | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Arabidopsis thaliana | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Schizosaccharomyces pombe | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Streptomyces coelicolor | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Oryza sativa | |
| ATP + acetyl-CoA + hydrogencarbonate = ADP + phosphate + malonyl-CoA | two-step reaction mechanism, structure-activity relationship | Toxoplasma gondii |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| adipose tissue | isozyme Acc1 | Mus musculus | - |
| adipose tissue | isozyme Acc1 | Homo sapiens | - |
| adipose tissue | isozyme Acc1 | Rattus norvegicus | - |
| brain | - |
Rattus norvegicus | - |
| heart | isozyme Acc2 | Mus musculus | - |
| heart | isozyme Acc2 | Homo sapiens | - |
| heart | isozyme Acc2 | Rattus norvegicus | - |
| liver | isozyme Acc1 | Mus musculus | - |
| liver | isozyme Acc1 | Homo sapiens | - |
| liver | isozyme Acc1 | Rattus norvegicus | - |
| mammary gland | lactating, isozyme Acc1 | Mus musculus | - |
| mammary gland | lactating, isozyme Acc1 | Homo sapiens | - |
| mammary gland | lactating, isozyme Acc1 | Rattus norvegicus | - |
| skeletal muscle | isozyme Acc2 | Mus musculus | - |
| skeletal muscle | isozyme Acc2 | Homo sapiens | - |
| skeletal muscle | isozyme Acc2 | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + acetyl-CoA + HCO3- | - |
Escherichia coli | ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | - |
Arabidopsis thaliana | ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | - |
Schizosaccharomyces pombe | ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | - |
Toxoplasma gondii | ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | biological function, overview | Hordeum vulgare | ADP + malonyl-CoA + phosphate | - |
? | |
| ATP + acetyl-CoA + HCO3- | biological function, overview | Oryza sativa | ADP + malonyl-CoA + phosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| ATP + acetyl-CoA + HCO3- | the enzyme is essential for viability | Saccharomyces cerevisiae | ADP + malonyl-CoA + phosphate | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| ATP + biotin + HCO3- | free biotin can be used as carboxyl acceptor with low activity | Escherichia coli | ADP + ? + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 265000, isozyme Acc1, 1 * 280000, isozyme Acc2 | Homo sapiens |
| More | a large, multi-domain enzyme | Hordeum vulgare |
| More | a large, multi-domain enzyme | Arabidopsis thaliana |
| More | a large, multi-domain enzyme | Schizosaccharomyces pombe |
| More | a large, multi-domain enzyme | Oryza sativa |
| More | a large, multi-domain enzyme, domain organization, structure analysis, overview | Saccharomyces cerevisiae |
| 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 |
| 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 |
| 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 |
| More | the alpha- and beta-subunits of the carboxyltransferase domain are shared with the propionyl-CoA carboxylase, EC 6.4.1.3 | Streptomyces coelicolor |
| oligomer | - |
Toxoplasma gondii |
| oligomer | subunit organization, overview | Streptomyces coelicolor |
| oligomer | subunit organization, structure analysis, overview | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ACC | - |
Mus musculus |
| ACC | - |
Escherichia coli |
| ACC | - |
Homo sapiens |
| ACC | - |
Rattus norvegicus |
| ACC | - |
Saccharomyces cerevisiae |
| ACC | - |
Hordeum vulgare |
| ACC | - |
Arabidopsis thaliana |
| ACC | - |
Schizosaccharomyces pombe |
| ACC | - |
Streptomyces coelicolor |
| ACC | - |
Oryza sativa |
| ACC | - |
Toxoplasma gondii |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Mus musculus |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Escherichia coli |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Homo sapiens |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Rattus norvegicus |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Saccharomyces cerevisiae |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Hordeum vulgare |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Arabidopsis thaliana |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Schizosaccharomyces pombe |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Streptomyces coelicolor |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Oryza sativa |
| More | the enzyme belongs to the family of biotin-dependent carboxylases | Toxoplasma gondii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mus musculus | |
| ATP | - |
Escherichia coli | |
| ATP | - |
Homo sapiens | |
| ATP | - |
Rattus norvegicus | |
| ATP | - |
Saccharomyces cerevisiae | |
| ATP | - |
Hordeum vulgare | |
| ATP | - |
Arabidopsis thaliana | |
| ATP | - |
Schizosaccharomyces pombe | |
| ATP | - |
Streptomyces coelicolor | |
| ATP | - |
Oryza sativa | |
| ATP | - |
Toxoplasma gondii | |
| biotin | dependent on | Schizosaccharomyces pombe | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Mus musculus | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Escherichia coli | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Homo sapiens | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Rattus norvegicus | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Saccharomyces cerevisiae | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Hordeum vulgare | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Arabidopsis thaliana | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Streptomyces coelicolor | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Oryza sativa | |
| biotin | dependent on, bound by the biotin carboxyl carrier protein | Toxoplasma gondii | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.000005 | - |
moiramide B | - |
Escherichia coli | |
IC50 Value
| IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
|---|---|---|---|---|---|
| 0.005 | 0.02 | IC50 of 0.005-0.02 mM | Toxoplasma gondii | FOP herbicides |
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