Cloned (Comment) | Organism |
---|---|
expression of the His-tagged biotinoyl domain in Escherichia coli strain AVB101 | Escherichia coli |
expression of wild-type and mutant His-tagged biotinoyl domains in Escherichia coli strain AVB101 | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
V927A/I931M/M932N/T933Q | site-directed mutagenesis, substitution of four amino acids in the vicinity of human MKM motif in analogy to the Escherichia coli biotinylation site | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Escherichia coli | |
Mg2+ | - |
Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + biotin-carboxyl-carrier protein + CO2 | Escherichia coli | - |
ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
ATP + biotin-carboxyl-carrier protein + CO2 | Homo sapiens | 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 | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene birA | - |
Homo sapiens | - |
contains isozymes ACC1 and ACC2 | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged biotinoyl domain from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration | Escherichia coli |
recombinant wild-type and mutant His-tagged biotinoyl domains from Escherichia coli strain AVB101 by nickel affinity chromatography and gel filtration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + biotin-carboxyl-carrier protein + CO2 | - |
Escherichia coli | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
ATP + biotin-carboxyl-carrier protein + CO2 | 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 | Homo sapiens | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
ATP + biotin-carboxyl-carrier protein + CO2 | 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 | Homo sapiens | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
ATP + biotin-carboxyl-carrier protein + CO2 | the biotinoyl domain interacts with the biotin-carboxyl-carrier protein, BCCP, biotin must be attached to ACC to produce a functional enzyme | Escherichia coli | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
additional information | mechanism of ACC holoenzyme function, structure of the biotinoyl domain of isozyme ACC2, overview | Homo sapiens | ? | - |
? | |
additional information | mechanism of ACC holoenzyme function, structure of the biotinoyl domain, overview. In thei BCCP, Glu 119 and Glu147 interact with the basic residues in BirA, overview | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | 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 | Homo sapiens |
More | geometry of the consensus Met-Lys-Met, MKM, motif, and structure of the biotinoyl domain of BCCP, overview. Binding pattern and interacting surfaces for the biotinoyl domain with BirA, overview | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
biotinoyl domain of acetyl-CoA carboxylase | - |
Homo sapiens |
BirA | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | ATP-dependent | Escherichia coli | |
ATP | ATP-dependent | Homo sapiens |