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Literature summary for 4.2.1.20 extracted from

  • Hiyama, T.; Sato, T.; Imanaka, T.; Atomi, H.
    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 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermococcus kodakarensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.035
-
indole pH 7.5, 85°C, he reaction is catalyzed by TrpB1 Thermococcus kodakarensis
0.0629
-
indole pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA Thermococcus kodakarensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
127000
-
2 * 27700 (alpha) + 2 * 67400 (beta), alpha,beta,beta,alpha heterotetramer, calculated from sequence Thermococcus kodakarensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate Thermococcus kodakarensis
-
L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q9YGB0 AND Q9YGA9 Q9YGB0: tryptophan synthase beta chain 1 (TrpB1), Q9YGA9: tryptophan synthase alpha chain (TrpA)
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate
-
Thermococcus kodakarensis L-tryptophan + D-glyceraldehyde 3-phosphate + H2O
-
?
L-serine + indole
-
Thermococcus kodakarensis L-tryptophan + H2O
-
?

Subunits

Subunits Comment Organism
heterotetramer alpha,beta,beta,alpha heterotetramer Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
TrpA TrpB1 and TrpA form a complex Thermococcus kodakarensis
TrpB1 TrpB1 and TrpA form a complex Thermococcus kodakarensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.04
-
indole pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA Thermococcus kodakarensis
3.46
-
indole pH 7.5, 85°C, he reaction is catalyzed by TrpB1 Thermococcus kodakarensis

General Information

General Information Comment Organism
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
metabolism the enzyme is involved in L-tryptophan 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, the reaction is catalyzed by the complex of TrpB1 and TrpA Thermococcus kodakarensis
99
-
indole pH 7.5, 85°C, he reaction is catalyzed by TrpB1 Thermococcus kodakarensis