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Literature summary for 4.1.3.27 extracted from

  • Baker, T.I.; Crawford, I.P.
    Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli (1966), J. Biol. Chem., 241, 5577-5584.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
L-Trp
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0012
-
 chorismate
-
 Escherichia coli
0.36
-
 glutamine
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate sequential mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.6
-
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chorismate + L-Gln
-
 Escherichia coli anthranilate + pyruvate + L-glutamate
-
 ?