The Enzyme Database

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Accepted name: anthranilate synthase
Reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
For diagram of tryptophan biosynthesis, click here
Other name(s): anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpE
Systematic name: chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
Comments: 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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-59-8
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 (1966) 5577–5584. [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 (1970) 365–380.
3.  Hütter, R., Niederberger, P. and DeMoss, J.A. Tryptophan synthetic genes in eukaryotic microorganisms. Annu. Rev. Microbiol. 40 (1986) 55–77. [PMID: 3535653]
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 (1969) 734–742. [PMID: 4886290]
5.  Zalkin, H. and Kling, D. Anthranilate synthetase. Purification and properties of component I from Salmonella typhimurium. Biochemistry 7 (1968) 3566–3573. [PMID: 4878701]
[EC created 1972]

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