EC Number | Cloned (Comment) | Organism |
---|---|---|
4.2.1.20 | expression in Escherichia coli | Thermococcus kodakarensis |
4.2.1.122 | expression in Escherichia coli | Thermococcus kodakarensis |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.20 | 0.035 | - |
indole | pH 7.5, 85°C, he reaction is catalyzed by TrpB1 | Thermococcus kodakarensis | |
4.2.1.20 | 0.0629 | - |
indole | pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA | Thermococcus kodakarensis | |
4.2.1.122 | 0.0081 | - |
indole | pH 7.5, 85°C | Thermococcus kodakarensis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.2.1.20 | 127000 | - |
2 * 27700 (alpha) + 2 * 67400 (beta), alpha,beta,beta,alpha heterotetramer, calculated from sequence | Thermococcus kodakarensis |
4.2.1.122 | 85600 | - |
gel filtration | Thermococcus kodakarensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.20 | L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | Thermococcus kodakarensis | - |
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
4.2.1.122 | L-serine + indole | Thermococcus kodakarensis | the enzyme is involved in L-tryptophan biosynthesis. TrpB2 does not interact with TrpA as in the case of TrpB1. TrpB2 provides an alternate route to generate Trp from serine and free indole (indole salvage) | L-tryptophan + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.1.20 | Thermococcus kodakarensis | Q9YGB0 AND Q9YGA9 | Q9YGB0: tryptophan synthase beta chain 1 (TrpB1), Q9YGA9: tryptophan synthase alpha chain (TrpA) | - |
4.2.1.122 | Thermococcus kodakarensis | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.2.1.20 | - |
Thermococcus kodakarensis |
4.2.1.122 | - |
Thermococcus kodakarensis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.2.1.20 | L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | - |
Thermococcus kodakarensis | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
4.2.1.20 | L-serine + indole | - |
Thermococcus kodakarensis | L-tryptophan + H2O | - |
? | |
4.2.1.122 | L-serine + indole | - |
Thermococcus kodakarensis | L-tryptophan + H2O | - |
? | |
4.2.1.122 | L-serine + indole | the enzyme is involved in L-tryptophan biosynthesis. TrpB2 does not interact with TrpA as in the case of TrpB1. TrpB2 provides an alternate route to generate Trp from serine and free indole (indole salvage) | Thermococcus kodakarensis | L-tryptophan + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.2.1.20 | heterotetramer | alpha,beta,beta,alpha heterotetramer | Thermococcus kodakarensis |
4.2.1.122 | dimer | 2 * 49300, calculated from sequence | Thermococcus kodakarensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.1.20 | TrpA | TrpB1 and TrpA form a complex | Thermococcus kodakarensis |
4.2.1.20 | TrpB1 | TrpB1 and TrpA form a complex | Thermococcus kodakarensis |
4.2.1.122 | TrpB2 | - |
Thermococcus kodakarensis |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.20 | 1.04 | - |
indole | pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA | Thermococcus kodakarensis | |
4.2.1.20 | 3.46 | - |
indole | pH 7.5, 85°C, he reaction is catalyzed by TrpB1 | Thermococcus kodakarensis | |
4.2.1.122 | 0.39 | - |
indole | pH 7.5, 85°C | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.2.1.20 | malfunction | double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAtrpB1 and DELTAtrpB2 strains) do not. To examine the capacity of TrpB1 and TrpB2 in Trp synthesis via indole salvage, DtrpEB1 and DtrpEB2 mutant strains are constructed using strain KUW1 (DELTApyrFDtrpE) as a host, eliminating the route for endogenous indole synthesis. Indole complements the Trp auxotrophies of DELTAtrpEB1 (DELTApyrFDELTAtrpEDELTAtrpB1) and DELTAtrpEB2 (DELTApyrFDELTAtrpEDELTAtrpB2) to similar levels. The results indicate that TrpB1 and TrpB2 both contribute to Trp biosynthesis in Thermococcus kodakarensis and can utilize free indole, and that indole salvage does not necessarily rely on TrpB2 to a greater extent | Thermococcus kodakarensis |
4.2.1.20 | metabolism | the enzyme is involved in L-tryptophan biosynthesis | Thermococcus kodakarensis |
4.2.1.122 | malfunction | double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAtrpB1 and DELTAtrpB2 strains) do not. To examine the capacity of TrpB1 and TrpB2 in Trp synthesis via indole salvage, DtrpEB1 and DtrpEB2 mutant strains are constructed using strain KUW1 (DELTApyrFDtrpE) as a host, eliminating the route for endogenous indole synthesis. Indole complements the Trp auxotrophies of DELTAtrpEB1 (DELTApyrFDELTAtrpEDELTAtrpB1) and DELTAtrpEB2 (DELTApyrFDELTAtrpEDELTAtrpB2) to similar levels. The results indicate that TrpB1 and TrpB2 both contribute to Trp biosynthesis in Thermococcus kodakarensis and can utilize free indole, and that indolesalvage does not necessarily rely on TrpB2 to a greater extent | Thermococcus kodakarensis |
4.2.1.122 | metabolism | the enzyme is involved in L-tryptophan biosynthesis | Thermococcus kodakarensis |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.2.1.20 | 17 | - |
indole | pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA | Thermococcus kodakarensis | |
4.2.1.20 | 99 | - |
indole | pH 7.5, 85°C, he reaction is catalyzed by TrpB1 | Thermococcus kodakarensis | |
4.2.1.122 | 48 | - |
indole | pH 7.5, 85°C | Thermococcus kodakarensis |