EC |
5.3.1.24 |
Accepted name: |
phosphoribosylanthranilate isomerase |
Reaction: |
N-(5-phospho-β-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate |
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For diagram of tryptophan biosynthesis, click here |
Other name(s): |
PRA isomerase; PRAI; IGPS:PRAI (indole-3-glycerol-phosphate synthetase/N-5′-phosphoribosylanthranilate isomerase complex); N-(5-phospho-β-D-ribosyl)anthranilate ketol-isomerase |
Systematic name: |
N-(5-phospho-β-D-ribosyl)anthranilate aldose-ketose-isomerase |
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 4.1.3.27 (anthranilate synthase) and EC 4.2.1.20 (tryptophan synthase)]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37259-82-8 |
References: |
1. |
Braus, G.H., Luger, K., Paravicini, G., Schmidheini, T., Kirschner, K. and Hütter, R. The role of the TRP1 gene in yeast tryptophan biosynthesis. J. Biol. Chem. 263 (1988) 7868–7875. [PMID: 3286643] |
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] |
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[EC 5.3.1.24 created 1990] |
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