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Literature summary for 6.3.4.14 extracted from
- Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis (2001), J. Biol. Chem., 276, 24991-24996.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| biotin | activates the ATP synthesis reaction with ADP and carbamoyl phosphate as substrates | Escherichia coli |  |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E276Q | kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP | Escherichia coli |
| H209A | kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP | Escherichia coli |
| K116A | kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP | Escherichia coli |
| K116Q | kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP | Escherichia coli |
| K159Q | kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Escherichia coli | |
| 0.19 | - |
ADP | pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate | Escherichia coli | |
| 4.8 | - |
Carbamoyl phosphate | pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate | Escherichia coli | |
| 125 | - |
biotin | pH 8, 25°C, K159Q mutant | Escherichia coli | |
| 134 | - |
biotin | wild-type enzyme | Escherichia coli | |
| 137 | - |
biotin | pH 8, 25°C, E276Q mutant | Escherichia coli | |
| 147 | - |
biotin | pH 8, 25°C, K116A mutant | Escherichia coli | |
| 1234 | - |
biotin | pH 8, 25°C, H209A mutant | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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]
| 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 | 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| 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 | catalytic mechanism | 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 | ? | |
| ATP + biotin + HCO3- | also uses free biotin as substrate | Escherichia coli | ADP + phosphate + carboxybiotin | - |
? | |
| 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 | - |
? | |
| 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 | |
| additional information | in the absence of biotin biotin carboxylase catalyzes a bicarbonate-dependent ATP hydrolysis at a slow rate | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 50000 | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| More | 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 |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | Lys-116, Lys-159, His-209 and Glu-276 are involved in ATP binding | Escherichia coli | |
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Release 2023.1 (January 2023)
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