Literature summary for 4.2.1.20 extracted from

Gualfetti, P.J.; Iwakura, M.; Lee, J.C.; Kihara, H.; Bilsel, O.; Zitzewitz, J.A.; Matthews, C.R.
Apparent radii of the native, stable intermediates and unfolded conformers of the alpha-subunit of tryptophan synthase from E. coli, a TIM barrel protein (1999), Biochemistry, 38, 13367-13378.

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
additional information	-	determination of Stoke's radii of native, stable intermediates and unfolded conformers of the purified recombinant alpha-subunit dependent on urea concentrations	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O	also catalyses the conversion of serine and indole into tryptophan and water, and of indoleglycerol phosphate into indole and glyceraldehyde phosphate (the latter reaction was listed formerly as EC 4.2.1.8)	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1-(indol-3-yl)glycerol 3-phosphate	alpha-subunit of the bienzyme complex, alpha-reaction	Escherichia coli	D-glyceraldehyde 3-phosphate + indole	-	?
L-serine + indole	beta-subunit of the bienzyme complex, beta-reaction	Escherichia coli	L-tryptophan + H2O	-	?

Subunits

Subunits	Comment	Organism
More	the alpha-subunit is a TIM barrel protein, structure analysis	Escherichia coli

Synonyms

Synonyms	Comment	Organism
alphaTS	-	Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	thermodynamic stability and kinetic	Escherichia coli

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Release 2023.1 (January 2023)