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Literature summary 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

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

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.20 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.20 alpha subunit Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.20 275
-
 indole + L-Ser Escherichia coli

Substrates and Products (Substrate)

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.20 0.0011
-
 indolebutanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage Escherichia coli
4.2.1.20 0.004
-
 indolepropanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage Escherichia coli
4.2.1.20 0.05
-
 indoleethanol phosphate competitive in the catalysis of indoleglycerol phosphate cleavage Escherichia coli