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Literature summary for 4.2.1.20 extracted from

  • Zhao, G.; Liu, J.; Dong, K.; Zhang, F.; Zhang, H.; Liu, Q.; Jiao, Q.
    Enzymatic synthesis of L-tryptophan from hair acid hydrolysis industries wastewater with tryptophan synthase (2011), Biores. Technol., 102, 3554-3557.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Tween-80 activates at 0.04% Escherichia coli

Application

Application Comment Organism
synthesis Recycling of hair by acid hydrolysis has enormous economic importance. Enzymatic synthesis of L-tryptophan from hair acid hydrolysis industries wastewater with tryptophan synthase. The L-serine conversion rate reaches 95.1% with a final L-tryptophan concentration of 33.2 g/l Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli strain BL21(DE3) Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme shows high tolerance to ammonium chloride from hair acid hydrolysis industries waste water, and shows no inhibition by ammonium chloride up to 75 mg/ml Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli MG1655
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + indole
-
Escherichia coli L-tryptophan + H2O
-
?
L-serine + indole
-
Escherichia coli MG1655 L-tryptophan + H2O
-
?

Synonyms

Synonyms Comment Organism
TSase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
recombinant enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
recombinant enzyme Escherichia coli