Literature summary for 4.2.1.20 extracted from

Xu, L.; Gao, G.; Cao, W.; Zhao, L.; Zhang, X.; Jiao, Q.; Chen, J.; Song, M.
Enzymatic synthesis of l-2-methyltryptophan catalyzed by tryptophan synthase in a water/organic solvent biphase system (2017), J. Food Sci. Biotechnol., 36, 547-552 .

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Application

Application	Comment	Organism
synthesis	synthesis of L-2-methyltryptophan L-serine and 2-methylindole by recombinant Escherichia coli with tryptophan synthase activity. Under the optimal conditions including 100 mmol/l L-serine, 100 mmol/l 2-methylindole, 1 g tryptophan synthase cells, 0.1mmol/l Ca2+, 50 ml reaction volume, 37ºC, pH 8.0, the bioconversion rate of L-2-methyltryptophan reaches 93% after 6 h	Escherichia coli

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-serine + 2-methylindole	-	Escherichia coli	L-2-methyltryptophan + H2O	-	?

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Release 2023.1 (January 2023)