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Literature summary for 4.2.1.20 extracted from

  • Dierkers, A.T.; Niks, D.; Schlichting, I.; Dunn, M.F.
    Tryptophan synthase: structure and function of the monovalent cation site (2009), Biochemistry, 48, 10997-11010.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.1.20

Metals/Ions

Metals/Ions Comment Organism Structure
Cs+
-
 Salmonella enterica subsp. enterica serovar Typhimurium
additional information without a bound monovalent cation both the reaction of indoline with alpha-aminoacrylate Schiff base species E(A-A) and the reaction with L-His with internal aldimine Schiff base species are strongly impaired. Monovalent cation binding ensures the structural integrity needed by the beta-active site during stage II of the beta-reaction Salmonella enterica subsp. enterica serovar Typhimurium
Na+
-
 Salmonella enterica subsp. enterica serovar Typhimurium
NH4+
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indoline + L-serine monovalent cation-bound alpha-aminoacrylate Schiff base species E(A-A) reacts rapidly with indoline to give the indoline quinonoid species, E(Q)indoline, which slowly converts to dihydroiso-L-tryptophan Salmonella enterica subsp. enterica serovar Typhimurium dihydroisotryptophan + H2O
-
 ?
L-histidine + L-serine reaction of L-His with internal aldimine species gives an equilibrating mixture of external aldimine and quinonoid species, E(Aex)his and E(Q)his Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?

Synonyms

Synonyms Comment Organism
tryptophan synthase
-
 Salmonella enterica subsp. enterica serovar Typhimurium