EC - Anthranilate synthase

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IntEnz Enzyme Nomenclature


Accepted name:
anthranilate synthase
Other names:
anthranilate synthetase
chorismate lyase
chorismate pyruvate-lyase (amino-accepting)
Systematic name:
chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)



In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC (anthranilate phosphoribosyltransferase ), EC (indole-3-glycerol-phosphate synthase), EC (tryptophan synthase) and EC (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00405
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004049
CAS Registry Number: 9031-59-8
UniProtKB/Swiss-Prot: (134) [show] [UniProt]


  1. Baker, T. and Crawford, I.P.
    Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli.
    J. Biol. Chem. 241: 5577-5584 (1966). [PMID: 5333199]
  2. Creighton, T.E. and Yanofsky, C.
    Chorismate to tryptophan (Escherichia coli) - anthranilate synthetase, PR transferase, PRA isomerase, InGP synthetase, tryptophan synthetase.
    Methods Enzymol. 17A: 365-380 (1970).
  3. Hütter, R., Niederberger, P. and DeMoss, J.A.
    Tryptophan biosynthetic genes in eukaryotic microorganisms.
    Annu. Rev. Microbiol. 40: 55-77 (1986).
  4. Ito, J. and Yanofsky, C.
    Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: Comparative studies on the complex and the subunits.
    J. Bacteriol. 97: 734-742 (1969). [PMID: 4886290]
  5. Zalkin, H. and Kling, D.
    Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium.
    Biochemistry 7: 3566-3573 (1968). [PMID: 4878701]

[EC created 1972]