This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin---[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
This enzyme, part of an acetyl-CoA carboxylase complex, acts on a biotin carboxyl-carrier protein (BCCP) that has been biotinylated by EC 6.3.4.15, biotin---[biotin carboxyl-carrier protein] ligase. In some organisms the enzyme is part of a multi-domain polypeptide that also includes the carrier protein (e.g. mycobacteria). Yet in other organisms (e.g. mammals) this activity is included in a single polypeptide that also catalyses the transfer of the carboxyl group from biotin to acetyl-CoA (see EC 6.4.1.2, acetyl-CoA carboxylase).
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview
biotin is covalently attached to a protein called the biotin-carboxyl-carrier protein. In mammals, these proteins comprise different domains in a single polypeptide chain, biotin must be attached to ACC to produce a functional enzyme
The overall acetyl-CoA carboxylase, ACC, reaction proceeds by a two-step mechanism. The first half-reaction is carried out by the biotin carboxylase and involves the ATP-dependent carboxylation of biotin, in which bicarbonate serves as the CO2 source. The carboxyl transferase catalyzes the second half-reaction in which the carboxyl group is transferred from biotin to acetyl-CoA to produce malonyl-CoA, the biotinoyl domain performs a critical function by transferring the activated carboxyl group from the biotin carboxylase domain to the carboxyl transferase domain, overview
macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Evaluation of pharmacokinetic/pharmacodynamic relationships of PD-0162819, a biotin carboxylase inhibitor representing a new class of antibacterial compounds, using in vitro infection models.
3D structure of the hACC2 biotinoyl domain, geometry of the consensus Met-Lys-Met, MKM, motif, overview. The biotin group of hACC2 does not affect the structure of the biotinoyl domain, the human enzyme does not possess a thumb structure. Binding pattern and interacting surfaces for the ACC2 biotinoyl domain with Escherichia coli BirA enzyme, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK
identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive
identification of mutations of the pyruvate carboxylase gene that cause pyruvate carboxylase deficiency. Deficiency form A results from association of two missense mutations located in biotin carboxylase or carboxyltransferase N-terminal part domains. Although most pyruvate carboxylase mutations are suggested to interfere with biotin metabolism, none of the pyruvate carboxylase-deficient patients tested is biotin-responsive