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Literature summary for 4.1.99.1 extracted from

  • Shimada, A.; Ozaki, H.; Saito, T.; Noriko, F.
    Tryptophanase-catalyzed L-tryptophan synthesis from D-serine in the presence of diammonium hydrogen phosphate (2009), Int. J. Mol. Sci., 10, 2578-2590.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.1.99.1

Activating Compound

Activating Compound Comment Organism Structure
diammonium hydrogen phosphate diammonium hydrogen phosphate serves as an activator on tryptophan synthesis from D-serine, maximum activity at 20% saturation concentration Escherichia coli
additional information NaCl, NH4H2PO4, NH4NO3, NH4Cl, (BH4)2CO3, K2HPO4, and Na2HPO4 have no effect on enzyme activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diammonium hydrogen phosphate diammonium hydrogen phosphate serves as an inhibitor of tryptophanase when L-serine is substrate, the activity decreases with increasing diammonium hydrogen phosphate Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-serine + indole the presence of 20% saturation concentration of diammonium hydrogen phosphate is required for this reaction Escherichia coli L-tryptophan + H2O
-
 ?
L-serine + indole
-
 Escherichia coli L-tryptophan + H2O
-
 ?
L-Trp + H2O
-
 Escherichia coli indole + pyruvate + NH4+
-
 ?
additional information tryptophanase displays no activity on D-tryptophan under usual conditions. However, it becomes active toward D-tryptophan degradation in highly concentrated diammonium hydrogen phosphate solutions Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
Tpase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli