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Literature summary for 4.2.1.20 extracted from

  • Buller, A.; Brinkmann-Chen, S.; Romney, D.; Herger, M.; Murciano-Calles, J.; Arnold, F.
    Directed evolution of the tryptophan synthase beta-subunit for stand-alone function recapitulates allosteric activation (2015), Proc. Natl. Acad. Sci. USA, 112, 14599-14604 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

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 [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

Organism UniProt Comment Textmining
Pyrococcus furiosus Q8U093 and Q8U094 Q8U093 i.e. subunit TrpB1, Q8U094 i.e. subunit TrpA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + indole
-
Pyrococcus furiosus L-tryptophan + H2O
-
?

Synonyms

Synonyms Comment Organism
TrpB1
-
Pyrococcus furiosus

Temperature Stability [°C]

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 [1/s]

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

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 [mM/s]

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