EC |
4.1.3.27 |
Accepted name: |
anthranilate synthase |
Reaction: |
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate |
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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 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (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 |
References: |
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. [DOI] [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] |
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[EC 4.1.3.27 created 1972] |
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