Literature summary for 4.2.1.20 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.

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Protein Variants

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

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

Reaction

Reaction	Comment	Organism	Reaction ID
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

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

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Release 2023.1 (January 2023)