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Literature summary for 2.4.2.18 extracted from

  • Ito, J.; Yanofsky, C.
    Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits (1969), J. Bacteriol., 97, 734-742.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
L-tryptophan transferase activity of component II is only inhibitable by L-tryptophan when the component is in the complex, this inhibition does not appear to depend upon the feedback-sensitive site of complex I Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
5-phospho-alpha-D-ribose 1-diphosphate complex Escherichia coli
0.2
-
5-phospho-alpha-D-ribose 1-diphosphate component II Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate Escherichia coli enzyme of tryptophan biosynthesis N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
anthranilate synthetase complex consisting of 2 separate subunits: component I and II
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
-
Escherichia coli N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
?
anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate enzyme of tryptophan biosynthesis Escherichia coli N-(5-phospho-D-ribosyl)-anthranilate + diphosphate
-
?