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Literature summary extracted from
- Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry (2001), J. Biol. Chem., 276, 11062-11071.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.2.1.20 | overexpression of the alpha-subunit in Escherichia coli | Pyrococcus furiosus |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 4.2.1.20 | purified recombinant alpha-subunit, hanging drop vapour diffusion method, 10°C, reservoir solution: 0.1 M MES-NaOH, pH 6.5, 12% PEG 20000, X-ray diffraction structure determination and analysis at 2.0 A resolution | Pyrococcus furiosus |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.2.1.20 | Pyrococcus furiosus | Q8U094 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.2.1.20 | recombinant alpha-subunit from Escherichia coli | Pyrococcus furiosus |
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) | Pyrococcus furiosus |
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 | Pyrococcus furiosus | D-glyceraldehyde 3-phosphate + indole | - |
? |  |
| 4.2.1.20 | L-serine + indole | beta-subunit of the bienzyme complex, beta-reaction | Pyrococcus furiosus | L-tryptophan + H2O | - |
? | |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.2.1.20 | additional information | - |
the alpha-subunit of the enzyme has extremely high thermostability, due to increase in ion pairs, decrease in cavity volume, and entropic effects, not by hydrophobic interactions | Pyrococcus furiosus |
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Release 2023.1 (January 2023)
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