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Literature summary for 4.1.99.1 extracted from
- Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase (2005), Biochemistry, 44, 14289-14297.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H463F | the rate constant for quinonoid intermediate formation from L-Trp is about 10fold lower for H463F Trpase than for wild-type Trpase, but the rate constant for reaction of L-Met is similar for H463F Trpase and wild-type Trpase | Escherichia coli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| L-Met | competitive | Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| mutant enzyme H463F | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-Trp + H2O | effects of temperature and hydrostatic pressure on the equilibria and rate constants for quinoid intermediate formation from L-Trp and L-Met with H463 mutant enzyme | Escherichia coli | indole + pyruvate + NH3 | - |
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