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Literature summary extracted from

  • Phillips, R.S.; Miles, E.W.; McPhie, P.; Marchal, S.; Lange, R.; Holtermann, G.; Goody, R.S.
    Effects of hydrostatic pressure on the conformational equilibrium of tryptophan synthase from Salmonella typhimurium (2010), Ann. N. Y. Acad. Sci., 1189, 95-103.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
4.2.1.20 D305A mutations that affects the allosteric equilibrium also has a dramatic effect on the reaction volume (DELTA V0) Salmonella enterica subsp. enterica serovar Typhimurium
4.2.1.20 E109D mutations that affects the allosteric equilibrium also has a dramatic effect on the reaction volume (DELTA V0) Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.1.20 L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O pressure perturbation is used to quantify the effects of monovalent cations, ligands, and mutations on the conformational equilibrium of Trp synthase. P-jump kinetics in the presence of Na+, NH4+, and Na+ together with benzimidazole are also examined. The plots of lnk versus P are nonlinear and require a compressibility (beta0) term to obtain a good fit. Compressibility (beta0) is positive for the Na+ enzyme but negative for NH4+ and Na+ with benzimidazole. These results suggest that there is a large contribution of solvation to the kinetics of the conformational change of Trp synthase Salmonella enterica subsp. enterica serovar Typhimurium
a

Synonyms

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