Protein Variants | Comment | Organism |
---|---|---|
E17G/I68V/F274S/T292S/T321A | mutation in subunit TrpB1, 50fold increase of catalytic efficiency of isolated beta subunit | Pyrococcus furiosus |
P12L/E17G/I68V/F274S/T292S/T321A | mutation in subunit TrpB1, 80fold increase of catalytic efficiency of isolated beta subunit | Pyrococcus furiosus |
T292S | mutation in subunit TrpB1, 20fold increase of catalytic efficiency of isolated beta subunit | Pyrococcus furiosus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.6 | - |
L-serine | wild-type holoenzyme, pH 8.0, 75°C | Pyrococcus furiosus | |
0.7 | - |
L-serine | subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus | |
0.84 | - |
L-serine | subunit TrpB1, mutant T292S, pH 8.0, 75°C | Pyrococcus furiosus | |
1.2 | - |
L-serine | subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus | |
1.2 | - |
L-serine | subunit TrpB1, wild-type, pH 8.0, 75°C | Pyrococcus furiosus | |
8.7 | - |
indole | subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus | |
11 | - |
indole | subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus | |
14 | - |
indole | subunit TrpB1, mutant T292S, pH 8.0, 75°C | Pyrococcus furiosus | |
20 | - |
indole | wild-type holoenzyme, pH 8.0, 75°C | Pyrococcus furiosus | |
77 | - |
indole | subunit TrpB1, wild-type, pH 8.0, 75°C | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | Q8U093 and Q8U094 | Q8U093 i.e. subunit TrpB1, Q8U094 i.e. subunit TrpA | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-serine + indole | - |
Pyrococcus furiosus | L-tryptophan + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TrpB1 | - |
Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
84 | - |
1 h, 50% residual activity, mutant E17G/I68V/F274S/T292S/T321A | Pyrococcus furiosus |
87 | - |
1 h, 50% residual activity, mutant P12L/E17G/I68V/F274S/T292S/T321A | Pyrococcus furiosus |
95 | - |
1 h, 50% residual activity, wild-type holoenzyme, wild-type subunit TrpB1 and mutant T292S | Pyrococcus furiosus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.31 | - |
indole | subunit TrpB1, wild-type, pH 8.0, 75°C | Pyrococcus furiosus | |
1 | - |
indole | wild-type holoenzyme, pH 8.0, 75°C | Pyrococcus furiosus | |
1.1 | - |
indole | subunit TrpB1, mutant T292S, pH 8.0, 75°C | Pyrococcus furiosus | |
2.2 | - |
indole | subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus | |
2.9 | - |
indole | subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus |
General Information | Comment | Organism |
---|---|---|
physiological function | as part of its native alphabetabetaalpha complex, subunit TrpB efficiently produces tryptophan and tryptophan analogs. Activity drops considerably when it is used as a stand-alone catalyst without the alpha-subunit. This lost activity can be recovered by mutations that reproduce the effects of complexation with the alpha-subunit | Pyrococcus furiosus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4 | - |
indole | subunit TrpB1, wild-type, pH 8.0, 75°C | Pyrococcus furiosus | |
50 | - |
indole | wild-type holoenzyme, pH 8.0, 75°C | Pyrococcus furiosus | |
78 | - |
indole | subunit TrpB1, mutant T292S, pH 8.0, 75°C | Pyrococcus furiosus | |
200 | - |
indole | subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus | |
330 | - |
indole | subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C | Pyrococcus furiosus |