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Literature summary for 4.2.1.20 extracted from
- The tryptophan synthase beta-subunit paralogs TrpB1 and TrpB2 in Thermococcus kodakarensis are both involved in tryptophan biosynthesis and indole salvage (2014), FEBS J., 281, 3113-3125.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21 cells | Thermococcus kodakarensis |
| expression in Escherichia coli | Thermococcus kodakarensis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0076 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA | Thermococcus kodakarensis |  |
| 0.0076 | - |
L-serine | subunit TrpB2 plus subunit TrpA, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 0.0081 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB1 | Thermococcus kodakarensis | |
| 0.0081 | - |
L-serine | subunit TrpB2, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 0.035 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA | Thermococcus kodakarensis | |
| 0.035 | - |
L-serine | subunit TrpB1 plus subunit TrpA, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 0.0629 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB2 | Thermococcus kodakarensis | |
| 0.629 | - |
L-serine | subunit TrpB1, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 20800 | - |
2 * 20800 + 2 * 67400, heterotetramer from subunits TrpA and TrpB1, SDS-PAGE | Thermococcus kodakarensis |
| 27700 | - |
2 * 27700 (subunit TrpA) + 2 * 42600 (subunit TrpB1), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1 | Thermococcus kodakarensis |
| 27700 | - |
2 * 27700 (subunit TrpA) + 2 * 49300 (subunit TrpB2), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1 | Thermococcus kodakarensis |
| 27700 | - |
2 * 27700 + 2 * 42600, heterotetramer from subunits TrpA and TrpB1, calculated from amino acid sequence | Thermococcus kodakarensis |
| 42600 | - |
2 * 27700 (subunit TrpA) + 2 * 42600 (subunit TrpB1), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1 | Thermococcus kodakarensis |
| 42600 | - |
2 * 27700 + 2 * 42600, heterotetramer from subunits TrpA and TrpB1, calculated from amino acid sequence | Thermococcus kodakarensis |
| 49300 | - |
2 * 27700 (subunit TrpA) + 2 * 49300 (subunit TrpB2), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1 | Thermococcus kodakarensis |
| 67400 | - |
2 * 20800 + 2 * 67400, heterotetramer from subunits TrpA and TrpB1, SDS-PAGE | Thermococcus kodakarensis |
| 140600 | - |
heterotetramer from subunits TrpA and TrpB1, calculated from amino acid sequence | Thermococcus kodakarensis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| indoleglycerol phosphate | Thermococcus kodakarensis | the reaction is catalyzed by the tryptophan synthase alpha-subunit TrpA | indole + D-glyceraldehyde 3-phosphate | - |
r | |
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | Thermococcus kodakarensis | overall reaction | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
ir | |
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | Thermococcus kodakarensis | the last two steps of L-tryptophan biosynthesis are catalyzed by Trp synthase, a heterotetramer composed of TrpA and TrpB. TrpB catalyzes the condensation of indole, synthesized by TrpA, and serine to Trp | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
| L-serine + indole | Thermococcus kodakarensis | the reaction is catalyzed by the tryptophan synthase beta-subunit paralogs TrpB1 and TrpB2 | L-tryptophan + H2O | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | - |
- |
- |
| Thermococcus kodakarensis | Q9YGA9 and Q5JDJ1 | Q9YGA9: alpha-subunit, Q5JDJ1: beta-subunit TrpB2 | - |
| Thermococcus kodakarensis | Q9YGA9 and Q9YGB0 | Q9YGA9: alpha-subunit, Q9YGB0: beta-subunit TrpB1 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermococcus kodakarensis |
| Resource 15 ISO column chromatography, Resource Q column chromatography, and Superdex 200 gel filtration | Thermococcus kodakarensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| indoleglycerol phosphate | the reaction is catalyzed by the tryptophan synthase alpha-subunit TrpA | Thermococcus kodakarensis | indole + D-glyceraldehyde 3-phosphate | - |
r | |
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | overall reaction | Thermococcus kodakarensis | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
ir | |
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | the last two steps of L-tryptophan biosynthesis are catalyzed by Trp synthase, a heterotetramer composed of TrpA and TrpB. TrpB catalyzes the condensation of indole, synthesized by TrpA, and serine to Trp | Thermococcus kodakarensis | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
| L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate | subunit TrpB catalyzes the condensation of indole, synthesized by subunit TrpA, and serine to Trp | Thermococcus kodakarensis | L-tryptophan + D-glyceraldehyde 3-phosphate + H2O | - |
? | |
| L-serine + indole | reaction is catalyzed by the beta-subunit, TrpB1 or TRpB2. TrpB1 is activated by the addition of the alpha-subunit TrpA and subsequent complex formation, whereas the activity of TrpB2 is not significantly affected by TrpA | Thermococcus kodakarensis | L-tryptophan + H2O | - |
? | |
| L-serine + indole | the reaction is catalyzed by the tryptophan synthase beta-subunit paralogs TrpB1 and TrpB2 | Thermococcus kodakarensis | L-tryptophan + H2O | - |
ir | |
| additional information | both subunit TrpB1 and TrpB2 show trace levels of serine deaminase activity by converting L-serine to pyruvate and ammonia | Thermococcus kodakarensis | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotetramer | 2 * 27700 (subunit TrpA) + 2 * 42600 (subunit TrpB1), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1 | Thermococcus kodakarensis |
| heterotetramer | 2 * 27700 (subunit TrpA) + 2 * 49300 (subunit TrpB2), calculated from sequence, tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1 | Thermococcus kodakarensis |
| heterotetramer | 2 * 20800 + 2 * 67400, heterotetramer from subunits TrpA and TrpB1, SDS-PAGE | Thermococcus kodakarensis |
| heterotetramer | 2 * 27700 + 2 * 42600, heterotetramer from subunits TrpA and TrpB1, calculated from amino acid sequence | Thermococcus kodakarensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Trp synthase | - |
Thermococcus kodakarensis |
| TrpB1 | tryptophan synthase beta-subunit paralog | Thermococcus kodakarensis |
| TrpB2 | tryptophan synthase beta-subunit paralog | Thermococcus kodakarensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 85 | - |
assay at | Thermococcus kodakarensis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.39 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB2 | Thermococcus kodakarensis | |
| 0.39 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA | Thermococcus kodakarensis | |
| 0.39 | - |
L-serine | subunit TrpB2 plus subunit TrpA, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 0.39 | - |
L-serine | subunit TrpB2, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 1.04 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB1 | Thermococcus kodakarensis | |
| 1.04 | - |
L-serine | subunit TrpB1, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 3.46 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA | Thermococcus kodakarensis | |
| 3.46 | - |
L-serine | subunit TrpB1 plus subunit TrpA, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Thermococcus kodakarensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | tryptophan synthase is composed of subunit TrpA and subunit TrpB. Thermococcus kodakarensis possess two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1. The double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAB1 and DELTAB2 strains) do not | Thermococcus kodakarensis |
| metabolism | the last two steps of L-tryptophan biosynthesis are catalyzed by Trp synthase, a heterotetramer composed of TrpA and TrpB. TrpB catalyzes the condensation of indole, synthesized by TrpA, and serine to Trp. Thermococcus kodakarensis possesses two paralogs of subunit B, TrpB1 and TrpB2. TrpB1 and TrpB2 both contribute to Trp biosynthesis | Thermococcus kodakarensis |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB1 | Thermococcus kodakarensis | |
| 17 | - |
L-serine | subunit TrpB2, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 48 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB2 | Thermococcus kodakarensis | |
| 48 | - |
L-serine | subunit TrpB1, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 51 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB2 in presence of subunit TrpA | Thermococcus kodakarensis | |
| 51 | - |
L-serine | subunit TrpB2 plus subunit TrpA, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
| 99 | - |
indole | pH 7.5, 85°C, reaction catalyzed by TrpB1 in presence of subunit TrpA | Thermococcus kodakarensis | |
| 99 | - |
L-serine | subunit TrpB1 plus subunit TrpA, at pH 7.5 and 85°C | Thermococcus kodakarensis | |
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