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Literature summary extracted from
- Biochemical analysis of a thermostable tryptophan synthase from a hyperthermophilic archaeon (2000), Eur. J. Biochem., 267, 6369-6377.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.20 | independent expression of alpha- and beta-subunit encoded by genes Tk-trpA and Tk-trpB in Escherichia coli | Thermococcus kodakarensis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.20 | Thermococcus kodakarensis | - |
hyperthermophilic archaeon, strain KOD1, alpha- and beta-subunit are encoded by genes Tk-trpA and Tk-trpB | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.20 | native enzyme complex, and recombinant alpha- and beta-subunit from expression in Escherichia coli | Thermococcus kodakarensis |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 4.2.1.20 | L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8) | Thermococcus kodakarensis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.20 | additional information | - |
activity of the prified recombinant individually expressed subunits is 10fold lower than the activity of the native enzyme complex | Thermococcus kodakarensis |
| 4.2.1.20 | 8.5 | - |
alpha-reaction, purified enzyme complex | Thermococcus kodakarensis |
| 4.2.1.20 | 110 | - |
overall activity, purified enzyme complex | Thermococcus kodakarensis |
| 4.2.1.20 | 119 | - |
beta-reaction, purified enzyme complex | Thermococcus kodakarensis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.2.1.20 | 1-(indol-3-yl)glycerol 3-phosphate | alpha-subunit of the bienzyme complex, alpha-reaction, the consumption of indole in the beta-reaction is necessary for optimal activity | Thermococcus kodakarensis | D-glyceraldehyde 3-phosphate + indole | - |
? |  |
| 4.2.1.20 | L-serine + indole | beta-subunit of the bienzyme complex, beta-reaction | Thermococcus kodakarensis | L-tryptophan + H2O | - |
? | |
| 4.2.1.20 | additional information | structure-activity relationship dependent on temperature for alpha- and beta-subunit | Thermococcus kodakarensis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.2.1.20 | dimer | recombinant beta-subunit, SDS-PAGE and gel filtration | Thermococcus kodakarensis |
| 4.2.1.20 | monomer | recombinant alpha-subunit, SDS-PAGE and gel filtration | Thermococcus kodakarensis |
| 4.2.1.20 | tetramer | alpha2beta2 enzyme complex, SDS-PAGE and gel filtration | Thermococcus kodakarensis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.20 | 70 | - |
alpha-reaction | Thermococcus kodakarensis |
| 4.2.1.20 | 80 | - |
overall reaction | Thermococcus kodakarensis |
| 4.2.1.20 | 90 | - |
beta-reaction | Thermococcus kodakarensis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.20 | 40 | 85 | recombinant alpha-subunit shows low activity at all temperatures | Thermococcus kodakarensis |
| 4.2.1.20 | 70 | 100 | recombinant beta-subunit, low activity below 70°C, increasing activity from 70°C to 100°C, at 100°C the activity is similar to the native enzyme complex | Thermococcus kodakarensis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.20 | additional information | - |
heat treatment for purification of the recombinant alpha- and beta-subunits, individually expressed, reveals that both the 2 subunits are required for stabilizationof the activity | Thermococcus kodakarensis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.20 | 7 | - |
alpha-and beta-reaction | Thermococcus kodakarensis |
| 4.2.1.20 | 8.5 | - |
overall reaction | Thermococcus kodakarensis |
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