EC Number | Application | Comment | Organism |
---|---|---|---|
6.3.4.14 | 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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
6.3.4.14 | overexpression system | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
6.3.4.14 | M169K | kinetic data, 5fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate | Escherichia coli |
6.3.4.14 | N290A | active site mutant, negative cooperativity with respect to bicarbonate | Escherichia coli |
6.3.4.14 | R338Q | kinetic data, 100fold lower Vmax than wild-type enzyme, negative cooperativity with respect to bicarbonate | Escherichia coli |
6.3.4.14 | R338S | kinetic data, 140fold lower catalytic efficiency than wild-type enzyme, negative cooperativity with respect to bicarbonate | Escherichia coli |
6.4.1.4 | M169K | mutant with lack of carboxylation activity | Escherichia coli |
6.4.1.4 | R338Q | mutant with lack of carboxylation activity | Escherichia coli |
6.4.1.4 | R338S | mutant with lack of carboxylation activity | Escherichia coli |
6.4.1.4 | R385S | human mutant leading to methylcrotonylglycinuria | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.4.14 | additional information | - |
additional information | kinetic data | Escherichia coli | |
6.3.4.14 | 25 | - |
biotin | R338S mutant | Escherichia coli | |
6.3.4.14 | 56 | - |
biotin | M169K mutant | Escherichia coli | |
6.3.4.14 | 134 | - |
biotin | wild-type enzyme | Escherichia coli | |
6.3.4.14 | 143 | - |
biotin | R338Q mutant | Escherichia coli | |
6.4.1.4 | 0.081 | - |
ATP | - |
Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
6.3.4.14 | Mg2+ | requirement | Escherichia coli | |
6.4.1.4 | Mg2+ | - |
Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
6.3.4.14 | 50000 | - |
2 * 50000, cooperativity between the subunits | Escherichia coli |
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 | 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 | - |
? | |
6.4.1.4 | ATP + acetyl-CoA + HCO3- | Escherichia coli | - |
ADP + malonyl-CoA + phosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
6.3.4.14 | Escherichia coli | - |
- |
- |
6.4.1.4 | Escherichia coli | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
6.3.4.14 | - |
Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
6.3.4.14 | ADP + carbamoyl phosphate | biotin carboxylase catalyzes the formation of ATP from ADP and carbamoyl phosphate | Escherichia coli | ATP + carbamate | - |
r | |
6.3.4.14 | ATP + biotin + HCO3- | utilizes free biotin as substrate | Escherichia coli | ADP + phosphate + carboxybiotin | - |
r | |
6.3.4.14 | 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 | - |
? | |
6.3.4.14 | 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 | |
6.3.4.14 | additional information | in absence of biotin enzyme also catalyzes a slow bicarbonate-dependent ATP hydrolysis | Escherichia coli | ? | - |
? | |
6.4.1.4 | ATP + acetyl-CoA + HCO3- | - |
Escherichia coli | ADP + malonyl-CoA + phosphate | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
6.3.4.14 | homodimer | 2 * 50000, cooperativity between the subunits | Escherichia coli |
6.4.1.4 | homodimer | alphabeta | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
6.4.1.4 | MCC | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
6.3.4.14 | 25 | - |
assay at | Escherichia coli |
6.3.4.14 | 37 | - |
assay at | Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
6.3.4.14 | additional information | - |
additional information | kinetic data | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
6.3.4.14 | 8 | - |
assay at | Escherichia coli |