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Literature summary for 6.3.4.14 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
Search for more literature for 6.3.4.14

Activating Compound

Activating Compound Comment Organism Structure
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)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli
0.08
-
 ADP pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
0.18
-
 ADP pH 8, 25°C, E211A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
0.23
-
 ADP pH 8, 25°C, E288A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
0.4
-
 ADP pH 8, 25°C, N290A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
0.51
-
 Carbamoyl phosphate pH 8, 25°C, E211A mutant, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
0.83
-
 ADP pH 8, 25°C, R292A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate Escherichia coli
2.3
-
 Carbamoyl phosphate pH 8, 25°C, E288A mutant, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
2.8
-
 Carbamoyl phosphate pH 8, 25°C, R292A mutant, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
11.2
-
 Carbamoyl phosphate pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate Escherichia coli
33.6
-
 biotin pH 8, 25°C, E211A mutant Escherichia coli
60.1
-
 biotin pH 8, 25°C, N290A mutant Escherichia coli
67.6
-
 biotin pH 8, 25°C, E288A mutant Escherichia coli
123.6
-
 biotin pH 8, 25°C, R292A mutant Escherichia coli
134
-
 biotin pH 8, 25°C, wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requires two equivalents of magnesium for activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 2 * 50000 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli JM109
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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 ?
ATP + biotin + HCO3- utilizes free biotin as substrate Escherichia coli ADP + phosphate + carboxybiotin
-
 ?
ATP + biotin + HCO3- utilizes free biotin as substrate Escherichia coli JM109 ADP + phosphate + carboxybiotin
-
 ?
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
-
 ?
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
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
-
 ?
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
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 ?
-
 ?
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

Subunits Comment Organism
homodimer 2 * 50000 Escherichia coli

Synonyms

Synonyms Comment Organism
More member of the ATP-grasp superfamily Escherichia coli

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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