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Literature summary for 4.2.1.20 extracted from

  • Fan, Y.X.; McPhie, P.; Miles, E.W.
    Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects (2000), Biochemistry, 39, 4692-4703.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
guanidinium i.e. GuH+, involved in the thermal stability and activity equilibrium of the enzyme complex, overview Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics and temperature-dependence Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
Cs+ involved in the thermal stability and activity equilibrium of the enzyme complex, overview Salmonella enterica subsp. enterica serovar Typhimurium
Na+ involved in the thermal stability and activity equilibrium of the enzyme complex, overview Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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) Salmonella enterica subsp. enterica serovar Typhimurium

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
190
-
wild-type enzyme, in presence of guanidinum Salmonella enterica subsp. enterica serovar Typhimurium
1310
-
wild-type enzyme, in presence of Na+ Salmonella enterica subsp. enterica serovar Typhimurium
1400
-
wild-type enzyme, in presence of Cs+ Salmonella enterica subsp. enterica serovar Typhimurium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
L-serine + indole beta-subunit of the bienzyme complex, beta-reaction Salmonella enterica subsp. enterica serovar Typhimurium L-tryptophan + H2O
-
?
additional information the intermediate product indole is transferred from the alpha- to the beta-site through a 25 A long hydrophobic tunnel Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?

Subunits

Subunits Comment Organism
More structure and conformation regulating the activity and allosteric communication in the enzyme complex, modeling of the high activity closed form and the low activity open form dependent on temperature, conversion from the open to the closed form at high temperature Salmonella enterica subsp. enterica serovar Typhimurium
tetramer alpha2beta2 complex Salmonella enterica subsp. enterica serovar Typhimurium

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5 50 thermodynamic analysis of the conformational change conditions and the effects of monovalent ions and effector DL-alpha-glycderol 3-phosphate Salmonella enterica subsp. enterica serovar Typhimurium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Salmonella enterica subsp. enterica serovar Typhimurium