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Literature summary for 4.2.1.20 extracted from

  • Kirschner, K.; Wiskocil, R.L.; Foehn, M.; Rezeau, L.
    The tryptophan synthase from Escherichia coli. An improved purification procedure for the alpha-subunit and binding studies with substrate analogues (1975), Eur. J. Biochem., 60, 513-523.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
indolebutanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.0011 mM Escherichia coli
indoleethanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.05 mM Escherichia coli
indolepropanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage, Ki: 0.004 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
alpha subunit Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
275
-
indole + L-Ser Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole + L-serine
-
Escherichia coli L-tryptophan + H2O
-
?
indole-3-glycerol phosphate
-
Escherichia coli indole + D-glyceraldehyde 3-phosphate
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0011
-
indolebutanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage Escherichia coli
0.004
-
indolepropanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage Escherichia coli
0.05
-
indoleethanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage Escherichia coli