Any feedback?
Literature summary for 6.3.4.14 extracted from
- Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin? (2000), Biochemistry, 39, 4122-4128.
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 |
|---|---|---|
| C230A | kinetic data, 50fold increased Km for ATP, no effect on the formation of carboxybiotin | Escherichia coli |
| K238Q | kinetic data, 50fold increased Km for ATP, no formation of carboxybiotin | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| N-ethylmaleimide | pH-dependent inhibition, reacts with Lys-238 | Escherichia coli | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Escherichia coli | |
| 0.081 | - |
ATP | 25°C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 0.37 | - |
HCO3- | 25°C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 0.7 | - |
HCO3- | 25°C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 4.23 | - |
ATP | 25°C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 6.87 | - |
ATP | 25°C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 122 | - |
biotin | 25°C, free biotin, wild-type enzyme | Escherichia coli | |
| 167 | - |
biotin | 25°C, free biotin, C230A 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 | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | long-chain fatty acid synthesis | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type and mutant enzymes | 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 | 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 utilizes free biotin as substrate | Escherichia coli | ADP + phosphate + carboxybiotin | - |
? | |
| ATP + biotin-carboxyl-carrier protein + HCO3- | one component of the multienzyme complex acetyl-CoA carboxylase, catalyzes the ATP-dependent carboxylation of biotin, for that biotin must be deprotonated at its N1 position, mechanism for deprotonation of biotin, bicarbonate is the source of CO2, Lys-238 plays a role in the carboxylation reaction, Cys-230 and Lys-238 do not act as an acid-base pair in the deprotonation of biotin, but may be involved in ATP binding | Escherichia coli | ADP + phosphate + carboxybiotin-carboxyl-carrier protein | - |
r | |
| additional information | long-chain fatty acid synthesis | Escherichia coli | ? | - |
? | |
| additional information | biotin carboxylase catalyzes a slow bicarbonate-dependent ATP hydrolysis reaction in the absence of biotin | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 50000 | 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 | |
| 0.0012 | - |
ATP | 25°C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 0.0017 | - |
ATP | 25°C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 0.00195 | - |
ATP | 25°C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin | Escherichia coli | |
| 0.513 | - |
ATP | 25°C, C230A mutant, biotin-dependent ATP hydrolysis | Escherichia coli | |
| 1.23 | - |
ATP | 25°C, wild-type enzyme, biotin-dependent ATP hydrolysis | Escherichia coli | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | ATP-dependent, Cys-230 and Lys-238 may be involved in binding ATP | Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
