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Literature summary for 6.3.4.14 extracted from
- Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: Evidence for cooperativity in biotin carboxylase (2004), J. Biol. Chem., 279, 15772-15778.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | the three biotin carboxylase mutants M169K, R338Q and R338S are used for study in order to mimic the disease-causing mutations M204K and R374Q of propionyl-CoA carboxylase and R385S of 3-methylcrotonyl-CoA carboxylase, which are mutations found in propionic acidemia or methylcrotonylglycinuria patients | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression system | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| M169K | kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate | Escherichia coli |
| N290A | active site mutant, negative cooperativity with respect to bicarbonate | Escherichia coli |
| R338Q | kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate | Escherichia coli |
| R338S | kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic data | Escherichia coli | |
| 25 | - |
biotin | R338S mutant | Escherichia coli |  |
| 56 | - |
biotin | M169K mutant | Escherichia coli | |
| 134 | - |
biotin | wild-type enzyme | Escherichia coli | |
| 143 | - |
biotin | R338Q mutant | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | requirement | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
2 * 50000, cooperativity between the subunits | 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 | biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ADP + carbamoyl phosphate | biotin carboxylase catalyzes the formation of ATP from ADP and carbamoyl phosphate | Escherichia coli | ATP + carbamate | - |
r | |
| ATP + biotin + HCO3- | utilizes free biotin as substrate | Escherichia coli | ADP + phosphate + carboxybiotin | - |
r | |
| ATP + biotin-carboxyl-carrier protein + HCO3- | biotin carboxylase catalyzes the first half-reaction in the first committed step in long chain fatty acid biosynthesis, catalyzed by acetyl-CoA carboxylase | Escherichia coli | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
? | |
| ATP + biotin-carboxyl-carrier protein + HCO3- | ATP-dependent carboxylation of biotin using bicarbonate as the carboxylate source, component of the multifunctional acetyl-CoA carboxylase, roles of Arg-338 and Lys-238 in the carboxyl transfer to biotin, Arg-338 serves to orient the carboxyphosphate intermediate for optimal carboxylation of biotin | Escherichia coli | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
r | |
| additional information | in absence of biotin enzyme also catalyzes a slow bicarbonate-dependent ATP hydrolysis | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 50000, cooperativity between the subunits | Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
| 37 | - |
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 | kinetic data | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
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