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Literature summary extracted from

  • Huang, Y.; You, W.; Caulkins, B.; Dunn, M.; Mueller, L.; Chang, C.
    Protonation states and catalysis Molecular dynamics studies of intermediates in tryptophan synthase (2016), Protein Sci., 25, 166-183 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.1.20 molecular dynamics simulations. The unprotonated pyridine nitrogen can form an H-bond with Ser377, which stabilizes the PLP ring structure. When the pyridoxyl phenolic oxygen is unprotonated, the polar side chain of Gln114 moves toward the negatively charged oxygen, which affects the movements of the water molecules around the active site and induces the switch to the open conformation of the beta subunit. The carboxylate oxygens typically form stable H-bonds with Thr110, Gly111, and His115 Salmonella enterica subsp. enterica serovar Typhimurium

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Salmonella enterica subsp. enterica serovar Typhimurium P00929 alpha-subunit
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4.2.1.20 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 P00929 alpha-subunit
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Synonyms

EC Number Synonyms Comment Organism
4.2.1.20 TrpA
-
 Salmonella enterica subsp. enterica serovar Typhimurium

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.1.20 pyridoxal 5'-phosphate in all intermediates, the unprotonated phosphoryl group with a formal -2 charge serves as the main anchor for the cofactor, maintaining important protein-substrate interactions and allowing for chemical transformations mediated by the functional groups of the PLP and substrates. The unprotonated pyridine nitrogen can form an H-bond with Ser377, which stabilizes the PLP ring structure Salmonella enterica subsp. enterica serovar Typhimurium