Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

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
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.20
-
Thermococcus kodakarensis
4.2.1.122
-
Thermococcus kodakarensis

Substrates and Products (Substrate)

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
-
?

Subunits

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

Synonyms

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

Turnover Number [1/s]

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

General Information

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

kcat/KM [mM/s]

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