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Literature summary for 4.1.99.1 extracted from

  • Fukui, S.; Ikeda, S.; Fujimura, M.
    Comparative studies on the properties of tryptophanase and tyrosine phenol-lyase immobilized directly on Sepharose or by use of Sepharose-bound pyridoxal 5 -phosphate (1975), Eur. J. Biochem., 51, 155-164.
    View publication on PubMed
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General Stability

General Stability Organism
immobilized enzyme shows higher thermal stability and resistance to a denaturing agent such as guanidine-HCl than the soluble enzyme Escherichia coli
when used repeatedly in a batch system or continously in a flow system in the absence of added pyridoxal 5'-phosphate, immobilized holo-tryptophanase gradually loses its original activity, pyridoxal 5'-phosphate restores its initial activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.33
-
 L-Trp
-
 Escherichia coli
0.34
-
 L-Trp immobilized enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli B/1t7-A
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Trp + H2O
-
 Escherichia coli indole + pyruvate + NH4+
-
 ?
L-Trp + H2O
-
 Escherichia coli B/1t7-A indole + pyruvate + NH4+
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 immobilized enzyme shows higher thermal stability Escherichia coli
55
-
 10 min, soluble enzyme is stable up to Escherichia coli
60
-
 10 min, immobilized enzyme is stable up to Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 9 immobilized enzyme Escherichia coli
8 10 soluble enzyme Escherichia coli