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Literature summary extracted from

  • Blanchard, C.Z.; Lee, Y.M.; Frantom, P.A.; Waldrop, G.L.
    Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin (1999), Biochemistry, 38, 3393-3400.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.14 biotin required for activation of the ATP synthesis reaction with carbamoyl phosphate and ADP as substrates, E211, E288, N290 and R292 are responsible, at least in part, for the substrate-induced synergism by biotin, activation via a conformational change of enzyme Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.14 expression in Escherichia coli BL21(DE3)pLysS Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.14 E211A 300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data Escherichia coli
6.3.4.14 E288A 300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data Escherichia coli
6.3.4.14 N290A 300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data Escherichia coli
6.3.4.14 R292A 300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data 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 0.08
-
 ADP pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
6.3.4.14 0.18
-
 ADP pH 8, 25°C, E211A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
6.3.4.14 0.23
-
 ADP pH 8, 25°C, E288A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
6.3.4.14 0.4
-
 ADP pH 8, 25°C, N290A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
6.3.4.14 0.51
-
 Carbamoyl phosphate pH 8, 25°C, E211A mutant, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
6.3.4.14 0.83
-
 ADP pH 8, 25°C, R292A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
6.3.4.14 2.3
-
 Carbamoyl phosphate pH 8, 25°C, E288A mutant, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
6.3.4.14 2.8
-
 Carbamoyl phosphate pH 8, 25°C, R292A mutant, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
6.3.4.14 11.2
-
 Carbamoyl phosphate pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
6.3.4.14 33.6
-
 biotin pH 8, 25°C, E211A mutant Escherichia coli
6.3.4.14 60.1
-
 biotin pH 8, 25°C, N290A mutant Escherichia coli
6.3.4.14 67.6
-
 biotin pH 8, 25°C, E288A mutant Escherichia coli
6.3.4.14 123.6
-
 biotin pH 8, 25°C, R292A mutant Escherichia coli
6.3.4.14 134
-
 biotin pH 8, 25°C, wild-type enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.14 Mg2+ requires two equivalents of magnesium for activity 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 biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- Escherichia coli JM109 biosynthesis of long-chain fatty acids, in vivo biotin is attached to the 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
-
-
-
6.3.4.14 Escherichia coli JM109
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.14 wild-type and mutant enzymes Escherichia coli

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 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 JM109 ATP + carbamate carbamate rapidly decomposes into carbon dioxide and ammonia ?
6.3.4.14 ATP + biotin + HCO3- utilizes free biotin as substrate Escherichia coli ADP + phosphate + carboxybiotin
-
 ?
6.3.4.14 ATP + biotin + HCO3- utilizes free biotin as substrate Escherichia coli JM109 ADP + phosphate + carboxybiotin
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- biosynthesis of long-chain fatty acids, in vivo biotin is attached to the 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- one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism Escherichia coli ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 r
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- biosynthesis of long-chain fatty acids, in vivo biotin is attached to the carboxyl-carrier protein through an amide bond to a specific lysine residue Escherichia coli JM109 ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 ?
6.3.4.14 ATP + biotin-carboxyl-carrier protein + HCO3- one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, active site structure, binding of biotin accelerates the rate of ATP hydrolysis about 1100fold: substrate-induced synergism Escherichia coli JM109 ADP + phosphate + carboxybiotin-carboxyl-carrier protein
-
 r
6.3.4.14 additional information in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin Escherichia coli ?
-
 ?
6.3.4.14 additional information in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATPase reaction at a 1100fold slower rate than in the presence of biotin Escherichia coli JM109 ?
-
 ?

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 member of the 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