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Literature summary extracted from

  • Ngo, H.; Kimmich, N.; Harris, R.; Niks, D.; Blumenstein, L.; Kulik, V.; Barends, T.R.; Schlichting, I.; Dunn, M.F.
    Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands (2007), Biochemistry, 46, 7740-7753.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.20 hanging drop vapour diffusion method Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.20 Cs+ the enzyme contains three Cs+ ions Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 Na+ in the presence of 100 mM NaCl the enzyme keeps in the Na+ activated form Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.20
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.20 L-serine + indole
-
 Salmonella enterica subsp. enterica serovar Typhimurium L-tryptophan + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.2.1.20 alpha2beta2 tryptophan synthase
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

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