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Literature summary for 4.2.1.20 extracted from

  • Weber-Ban, E.; Hur, O.; Bagwell, C.; Banik, U.; Yang, L.H.; Miles, E.W.; Dunn, M.F.
    Investigation of allosteric linkages in the regulation of tryptophan synthase: the roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics (2001), Biochemistry, 40, 3497-3511.
    View publication on PubMed
Search for more literature for 4.2.1.20

Protein Variants

Protein Variants Comment Organism
D305N site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview Salmonella enterica subsp. enterica serovar Typhimurium
D56A site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview Salmonella enterica subsp. enterica serovar Typhimurium
K167T site-directed mutagenesis, residue is involved in formation of salt bridges between the different subunits, kinetic and structural, conformational alterations, altered signaling by ligand binding, overview Salmonella enterica subsp. enterica serovar Typhimurium

Inhibitors

Inhibitors Comment Organism Structure
DL-glycerol 3-phosphate inhibits beta-reaction activity of wild-type and mutant D56A Salmonella enterica subsp. enterica serovar Typhimurium
K+ inhibits mutant D56A beta-reaction activity, inhibits alpha-reaction of all wild-type and mutants, enhances the overall enzyme complex activity for all wild-type and mutant enzymes, except for mutant D56A Salmonella enterica subsp. enterica serovar Typhimurium
Na+ inhibits beta-reaction activity of mutant D56A, D305N and K167T, inhibits alpha-reaction of wild-type and mutant D56A, enhances the overall enzyme complex activity for all wild-type and mutant enzymes except for mutant D56A Salmonella enterica subsp. enterica serovar Typhimurium
NH4+ inhibits mutant D56A, D305N and K167T alpha-reaction activity, inhibits alpha-reaction of wild-type and mutant D56A, enhances the overall enzyme complex activity for all wild-type and mutant enzymes 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, wild-type and mutants, isotope effects and effector influence Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
DL-glycerol 3-phosphate enhances beta-reaction activity of mutant D305N and K167T Salmonella enterica subsp. enterica serovar Typhimurium
K+ enhances beta-reaction activity of wild-type and mutants, except for mutant D56A Salmonella enterica subsp. enterica serovar Typhimurium
Na+ enhances beta-reaction activity of wild-type Salmonella enterica subsp. enterica serovar Typhimurium
NH4+ enhances beta-reaction activity of all wild-type and mutants 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), catalytic mechanism Salmonella enterica subsp. enterica serovar Typhimurium
a

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 allostery and substrate channeling, synergism between binding interactions at the monovalent cation binding site, the formation of salt bridges to support allosteric communication between sites, ligand binding to the alpha-site, and the catalytic activities of the alpha- and beta-sites Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?

Subunits

Subunits Comment Organism
More structure models Salmonella enterica subsp. enterica serovar Typhimurium
tetramer alpha2beta2 enzyme complex Salmonella enterica subsp. enterica serovar Typhimurium