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Literature summary extracted from

  • Thoden, J.B.; Blanchard, C.Z.; Holden, H.M.; Waldrop, G.L.
    Movement of the biotin carboxylase B-domain as a result of ATP binding (2000), J. Biol. Chem., 275, 16183-16190.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.14 X-ray structure, native and E288K mutant enzyme, both complexed with ATP Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.14 E288K mutant with completely abolished ability to hydrolyze ATP Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.14 Mg2+ requirement Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.14 additional information Escherichia coli fatty acid synthesis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.14 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.14 native and E288K mutant enzyme Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.4.14 ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine reaction mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.14 ATP + biotin + HCO3- also utilizes free biotin as substrate Escherichia coli ADP + phosphate + carboxybiotin
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- biotin carboxylase is one of three distinct components of acetyl-CoA carboxylase, carboxylation of the ureido ring of biotin at the N-1 position, reaction mechanism, domain structure, the biotin carboxylase B-domain moves as a result of ATP binding, enzyme structure Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 r
6.3.4.14 additional information fatty acid synthesis Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.14 dimer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.3.4.14 More belongs to the ATP-grasp superfamily Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.14 ATP ATP-dependent, mode of binding, Lys-116, His-236 and Glu-201 are involved in binding ATP, the biotin carboxylase B-domain moves as a result of ATP binding Escherichia coli