4.2.1.122: tryptophan synthase (indole-salvaging)
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For detailed information about tryptophan synthase (indole-salvaging), go to the full flat file.
Reaction
Synonyms
PfTrpB, PfTrpS, StTrpS (beta2), Trp synthase, TrpB2, TrpBbeta, TRPS, tryptophan synthase
ECTree
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General Information on EC 4.2.1.122 - tryptophan synthase (indole-salvaging)
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
the double-deletion mutant (DELTAtrpB1DELTAtrpB2) displays Trp auxotrophy, whereas individual single mutants (DELTAtrpB1 and DELTAtrpB2 strains) does not
malfunction
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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
metabolism
the last two steps of L-tryptophan (Trp) 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. TrpB2 catalyzes the TrpB reaction but does not interact with TrpA as in the case of TrpB1. TrpB1 and TrpB2 both contribute to Trp biosynthesis in Thermococcus kodakarensis and can utilize free indole, and indole salvage does not necessarily rely on TrpB2 to a greater extent
physiological function
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TrpB2 acts as an indole rescue protein, which prevents the escape of this costly hydrophobic metabolite from the cell at the high growth temperatures of hyperthermophiles
physiological function
trpB2 contributes in Trp biosynthesis
physiological function
the enzyme is part of the tryptophan synthase complex. Indole formation is catalyzed by the alpha-subunit (TrpBalpha), L-tryptophan production is catalyzed by the beta-subunit (TrpBbeta)
physiological function
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tryptophan synthase (TrpS) catalyzes the final steps in the biosynthesis of L-tryptophan from L-serine (Ser) and indole-3-glycerol phosphate (IGP). Native TrpS can also catalyze a productive reaction with L-threonine (Thr), leading to (2S,3S)-beta-methyltryptophan
additional information
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leucine residue Leu166 (betaL166) is in close proximity to the beta-position of the alpha-aminoacrylate species
additional information
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leucine residue Leu166 (betaL166) is in close proximity to the beta-position of the alpha-aminoacrylate species
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