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Literature summary for 6.3.4.14 extracted from

  • Lee, C.K.; Cheong, H.K.; Ryu, K.S.; Lee, J.I.; Lee, W.; Jeon, Y.H.; Cheong, C.
    Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism (2008), Proteins, 72, 613-624.
    View publication on PubMed

Cloned(Commentary)

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

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

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli
Mg2+
-
Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Escherichia coli
-
gene birA
-
Homo sapiens
-
contains isozymes ACC1 and ACC2
-

Purification (Commentary)

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 and Products (Substrate)

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

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

Synonyms Comment Organism
biotinoyl domain of acetyl-CoA carboxylase
-
Homo sapiens
BirA
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP ATP-dependent Escherichia coli
ATP ATP-dependent Homo sapiens