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Literature summary extracted from

  • Sloane, V.; Blanchard, C.Z.; Guillot, F.; Waldrop, G.L.
    Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis (2001), J. Biol. Chem., 276, 24991-24996.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.14 biotin activates the ATP synthesis reaction with ADP and carbamoyl phosphate as substrates Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.14 E276Q kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP Escherichia coli
6.3.4.14 H209A kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP Escherichia coli
6.3.4.14 K116A kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP Escherichia coli
6.3.4.14 K116Q kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP Escherichia coli
6.3.4.14 K159Q kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.14 additional information
-
 additional information
-
 Escherichia coli
6.3.4.14 0.19
-
 ADP pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
6.3.4.14 4.8
-
 Carbamoyl phosphate pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
6.3.4.14 125
-
 biotin pH 8, 25°C, K159Q mutant Escherichia coli
6.3.4.14 134
-
 biotin wild-type enzyme Escherichia coli
6.3.4.14 137
-
 biotin pH 8, 25°C, E276Q mutant Escherichia coli
6.3.4.14 147
-
 biotin pH 8, 25°C, K116A mutant Escherichia coli
6.3.4.14 1234
-
 biotin pH 8, 25°C, H209A mutant Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.14 Mg2+ requires two equivalents of magnesium for activity, one is complexed to ATP, the role of the other is unknown Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.4.14 50000
-
 2 * 50000 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 ATP + biotin-carboxyl-carrier protein + HCO3- Escherichia coli long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.14 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 catalytic mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.14 ADP + carbamoyl phosphate biotin carboxylase catalyzes an ATP synthesis reaction, in which a phosphate group is transferred from carbamoyl phosphate to ADP forming ATP and carbamate Escherichia coli ATP + carbamate carbamate rapidly decomposes into carbon dioxide and ammonia ?
6.3.4.14 ATP + biotin + HCO3- also uses free biotin as substrate Escherichia coli ADP + phosphate + carboxybiotin
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- long-chain fatty acid synthesis, in vivo biotin is linked to the biotin-carboxyl-carrier protein through an amide bond to a specific lysine residue Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- the biotin carboxylase component of acetyl-CoA carboxylase catalyzes the ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding and in catalysis orienting ATP in a conformation that allows for optimal catalysis, mechanism Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 r
6.3.4.14 additional information in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATP hydrolysis at a slow rate Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.4.14 homodimer 2 * 50000 Escherichia coli

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.14 25
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.4.14 additional information
-
 additional information
-
 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.14 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.14 ATP Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding Escherichia coli