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Literature summary for 4.1.99.1 extracted from

  • Watanabe, T.; Snell, E.E.
    Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia (1972), Proc. Natl. Acad. Sci. USA, 69, 1086-1090.
    View publication on PubMedView publication on EuropePMC
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.019
-
 indole
-
 Escherichia coli
70
-
 pyruvate
-
 Escherichia coli
345
-
 NH4+
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-tryptophan + H2O = indole + pyruvate + NH3 in the reverse direction NH4+ interacts with bound pyridoxal 5'-phosphate to form an imine. Pyruvate is the second substrate, indole the third. alpha-Aminoacrylate functions as a common enzyme-bound intermediate in both synthetic and degradative reactions Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole + pyruvate + NH4+
-
 Escherichia coli L-Trp + H2O
-
 ?
L-Trp + H2O
-
 Escherichia coli indole + pyruvate + NH4+
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 degradation of Trp Escherichia coli
9
-
 synthesis of Trp Escherichia coli