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