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Literature summary for 4.1.99.1 extracted from
- Effects of temperature and monovalent cations on activity and quaternary structure of tryptophanase (1986), J. Biochem., 100, 679-685.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | promotes the conversion of the inactive holoenzyme into the active holoenzyme rather than being involved in the conversion of the apoenzyme and pyridoxal 5'-phosphate into the active holoenzyme | Escherichia coli |  |
| NH4+ | promotes the conversion of the inactive holoenzyme into the active holoenzyme rather than being involved in the conversion of the apoenzyme and pyridoxal 5'-phosphate into the active holoenzyme | Escherichia coli | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-Trp + H2O | - |
Escherichia coli | indole + pyruvate + NH4+ | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 5 | - |
stable in presence of K+, gradual loss of activity in absence of K+ | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Escherichia coli | |
| pyridoxal 5'-phosphate | conversion of apoenzyme into the active holoenzyme is attained at 30°C in Tris-HCl buffer, pH 8.0, containing pyridoxal 5'-phosphate and K+, no conversion occurs at 5°C | Escherichia coli | |
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