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Literature summary extracted from

  • Barends, T.R.; Dunn, M.F.; Schlichting, I.
    Tryptophan synthase, an allosteric molecular factory (2008), Curr. Opin. Chem. Biol., 12, 593-600.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.2.8
-
Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

EC Number Protein Variants Comment Organism
4.1.2.8 Q114N betaGln114Asn mutation, which shortens the betaGln114 side chain connecting the betaL3 loop with the rest of the protein, resulted in two fractions of enzyme Salmonella enterica subsp. enterica serovar Typhimurium
4.1.2.8 Y110V betaThr110Val mutation, which replaces a hydrogen bonding partner to the substrate carboxylate with a methyl group severely decreased the ability to form the aminoacrylate external aldimine E(AA) and consequently severely impaired beta-reaction and alphabeta-reaction Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.8 indole-3-glycerol phosphate alpha-site cleaves the C3-C30 bond of IGP Salmonella enterica subsp. enterica serovar Typhimurium indole + D-glyceraldehyde 3-phosphate
-
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Subunits

EC Number Subunits Comment Organism
4.1.2.8 dimer TrpS alphabeta-dimer Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

EC Number Synonyms Comment Organism
4.1.2.8 TRPS
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Salmonella enterica subsp. enterica serovar Typhimurium