Cloned (Comment) | Organism |
---|---|
recombinant enzyme expression in Escherichia coli strain JM101 | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
(S)-4-(benzimidazol-1-yl)-2-aminobutanoic acid | - |
Escherichia coli | |
2,3-dihydro-L-tryptophan | - |
Escherichia coli | |
2-oxindolyl-L-alanine | - |
Escherichia coli | |
L-bishomotryptophan | potent inhibitor, formation of an external aldimine. The compound is a selective inhibitor and is a potential lead for the development of antibacterials | Escherichia coli | |
L-homotryptophan | a moderate competitive inhibitor, formation of an external aldimine and quinonoid | Escherichia coli | |
L-tryptophan | weak substrate inhibition | Escherichia coli | |
additional information | design, synthesis, and evaluation of homotryptophan analogues as possible mechanism-based inhibitors for Escherichia coli tryptophan indole-lyase, overview. As a quinonoid structure is an intermediate in the reaction mechanism of TIL, homologation of the physiological substrate, L-Trp, might provide analogues resembling the transition state for beta-elimination, and potentially inhibit the enzyme. Kinetics show that formation of a quinonoid complex is not required for strong inhibition | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tryptophan + H2O | Escherichia coli | - |
indole + pyruvate + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A853 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme from Escherichia coli strain JM101 | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-tryptophan + H2O = indole + pyruvate + NH3 | proposed mechanism of tryptophan indole-lyase, overview | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-tryptophan + H2O | - |
Escherichia coli | indole + pyruvate + NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TIL | - |
Escherichia coli |
tryptophan indole-lyase | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | dependent on | Escherichia coli |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | pre-steady-state inhibition kinetics, rapid-scanning stopped-flow experiments | Escherichia coli | |
0.002 | - |
2,3-dihydro-L-tryptophan | pH 8.0, 25°C, recombinant enzyme | Escherichia coli | |
0.0047 | - |
L-bishomotryptophan | pH 8.0, 25°C, recombinant enzyme | Escherichia coli | |
0.005 | - |
2-oxindolyl-L-alanine | pH 8.0, 25°C, recombinant enzyme | Escherichia coli | |
0.013 | - |
(S)-4-(benzimidazol-1-yl)-2-aminobutanoic acid | pH 8.0, 25°C, recombinant enzyme | Escherichia coli | |
0.067 | - |
L-homotryptophan | pH 8.0, 25°C, recombinant enzyme | Escherichia coli | |
0.2 | - |
L-tryptophan | pH 8.0, 25°C, recombinant enzyme | Escherichia coli |