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Literature summary extracted from

  • Schiaretti, F.; Bettati, S.; Viappiani, C.; Mozzarelli, A.
    pH dependence of tryptophan synthase catalytic mechanism. I. The first stage, the beta-elimination reaction (2004), J. Biol. Chem., 279, 29572-29582.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.20 additional information
-
 additional information kinetics, beta-reaction Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.20 additional information the beta-reaction is influenced by protons, monovalent cations, and alpha-subunit ligands, that modulate the distribution between open and closed conformation Salmonella enterica subsp. enterica serovar Typhimurium

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8), detailed mechanism of the beta-reaction, beta-active site structure Salmonella enterica subsp. enterica serovar Typhimurium
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.20 1-(indol-3-yl)glycerol 3-phosphate alpha-subunit of the bienzyme complex, alpha-reaction Salmonella enterica subsp. enterica serovar Typhimurium D-glyceraldehyde 3-phosphate + indole
-
 ?
4.2.1.20 L-serine + indole beta-subunit of the bienzyme complex, beta-reaction, first step of the reaction is a beta-elimination taht involves a very fast interconversion of the internal aldimine in a highly fluorescent L-serine external aldimine that decays to the alpha-aminoacrylate Schiff base via the alpha-carbon proton removal and beta-hydroxyl group release Salmonella enterica subsp. enterica serovar Typhimurium L-tryptophan + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.20 tetramer alpha2beta2 enzyme complex Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

EC Number Synonyms Comment Organism
4.2.1.20 TS
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.20 20
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.20 additional information
-
 pH-profiling, pH-dependence of the beta-reaction in absence or presence of Na+, Cs+, K+, influence of monovalent cations in combination with alpha-subunit ligand indole-acetylglycine, overview Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 6 9 beta-reaction is biphasic Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.20 pyridoxal 5'-phosphate dependent on, bound via Schiff base to beta-subunit residue Lys87 Salmonella enterica subsp. enterica serovar Typhimurium