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Literature summary extracted from

  • Balderas-Hernandez, V.E.; Sabido-Ramos, A.; Silva, P.; Cabrera-Valladares, N.; Hernandez-Chavez, G.; Baez-Viveros, J.L.; Martinez, A.; Bolivar, F.; Gosset, G.
    Metabolic engineering for improving anthranilate synthesis from glucose in Escherichia coli (2009), Microb. Cell Fact., 8, 19.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
4.1.3.27 biotechnology development of a microbial system for the environmentally-compatible synthesis of anthranilate generated by metabolic engineering of trpD gene from strain W3110 trpD9923 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.27 Escherichia coli
-
 W3110 trpD9923
-
4.1.3.27 Escherichia coli W3110 trpD9923
-
 W3110 trpD9923
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.27 chorismate + L-glutamine
-
 Escherichia coli anthranilate + pyruvate + L-glutamate
-
 ?
4.1.3.27 chorismate + L-glutamine
-
 Escherichia coli W3110 trpD9923 anthranilate + pyruvate + L-glutamate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.3.27 anthranilate synthase
-
 Escherichia coli
4.1.3.27 TrpED
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
4.1.3.27 malfunction mutation in strain trpD9923 (mutant in the tryptophan operon) results in the synthesis of a truncated anthranilate synthase component II protein, retaining the full glutamine amidotransferase domain and only seven of the 333 amino acid residues of the anthranilate phosphoribosyl transferase domain. Mutation in the trpD gene causes the loss of anthranilate phosphoribosyl transferase activity, but maintains anthranilate synthase activity, thus causing anthranilate accumulation Escherichia coli