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Literature summary for 6.3.4.14 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
Search for more literature for 6.3.4.14

Crystallization (Commentary)

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

Protein Variants

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + HCO3- also utilizes free biotin as substrate Escherichia coli ADP + phosphate + carboxybiotin
-
 ?
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
additional information fatty acid synthesis Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Escherichia coli

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
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