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 (Comment) | Organism |
---|---|
expression in Escherichia coli BL21(DE3)pLysS | Escherichia coli |
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 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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | requires two equivalents of magnesium for activity | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
50000 | - |
2 * 50000 | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Escherichia coli JM109 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
wild-type and mutant enzymes | Escherichia coli |
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 | Comment | Organism |
---|---|---|
homodimer | 2 * 50000 | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
More | member of the ATP-grasp superfamily | Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |