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Chemical Compound Review

IGPS     [2,3-dihydroxy-3-(1H-indol- 3...

Synonyms: AG-J-16516, SureCN2291738, CHEBI:18299, AC1Q6RYM, CTK4I5857, ...
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Disease relevance of indole-3-glycerol-P


High impact information on indole-3-glycerol-P

  • By combining an existing binding site for structural elements of phosphoribosylanthranilate with a catalytic template required for isomerase activity, we are able to evolve phosphoribosylanthranilate isomerase activity from the scaffold of indole-3-glycerol-phosphate synthase [6].
  • Based on the mutant phenotypes, we propose that a particular sequence of protein--protein and protein--DNA interactions is required for activation of trpPB by TrpI and InGP [7].
  • Our hypothesis holds that the trpA type of "indole-utilization" mutation alters the repressor (synthase alpha-chain) so that indole as well as indole-3-glycerol-P serves as an effector molecule for tryptophan synthase induction [8].
  • We propose that the alpha-chain of the synthase has an autogenous regulatory function, serving as the repressor or the indole-3-glycerol-P recognition component of the repressor of the trpAB operon (synthase alpha-and beta-chains) [8].
  • According to the kinetic parameters of the purified isomerase protein, the enzyme is more active than, for example, the purified TRP3 enzyme indoleglycerol-phosphate synthase [9].

Chemical compound and disease context of indole-3-glycerol-P


Biological context of indole-3-glycerol-P


Associations of indole-3-glycerol-P with other chemical compounds


Gene context of indole-3-glycerol-P

  • It is suggested that the TRP1 gene of Saccharomyces cerevisiae might be the result of a rearrangement event, separating the N-(5'-phosphoribosyl-1)-anthranilate isomerase domain from the indoleglycerol-phosphate synthase domain and putting the catalytically more active isomerase domain behind a weak and nonregulated constitutive promoter [9].
  • The results show that four of the five activities examined are stable under most nongrowing conditions, whereas one activity, indoleglycerol phosphate (InGP) synthetase, carried by the trpC protein, is unstable under most conditions tested [22].
  • The Pseudomonas aeruginosa tryptophan synthase genes, trpA and trpB, which are induced by their substrate indoleglycerol phosphate, were cloned along with their controlling region into the BamHI site of pBR322 to produce the 10.7-megadalton plasmid pZAZ5 [23].
  • Expression of the trpBA gene pair of Pseudomonas aeruginosa is regulated by the endogenous level of indoleglycerol phosphate (InGP) and the trpI gene product [24].
  • The majority of the enzymatically defective mutant alpha subunits have decreased capacities for substrate (indole-3-glycerol phosphate) utilization, typical of the early trpA missense mutants isolated by in vivo selection methods [25].

Analytical, diagnostic and therapeutic context of indole-3-glycerol-P


  1. Partly native epitopes are already present on early intermediates in the folding of tryptophan synthase. Blond, S., Goldberg, M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  2. The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges. Knöchel, T., Pappenberger, A., Jansonius, J.N., Kirschner, K. J. Biol. Chem. (2002) [Pubmed]
  3. The roles of indoleglycerol phosphate and the TrpI protein in the expression of trpBA from Pseudomonas aeruginosa. Chang, M., Crawford, I.P. Nucleic Acids Res. (1990) [Pubmed]
  4. Sequence of the indoleglycerol phosphate synthase (trpC) gene from Rhodobacter capsulatus. Becker-Rudzik, M., Young, D.A., Marrs, B.L. J. Bacteriol. (1992) [Pubmed]
  5. Amino-terminal sequences of indoleglycerol phosphate synthetase of Escherichia coli and Salmonella typhimurium. Li, S.S., Hanlon, J., Yanofsky, C. J. Bacteriol. (1975) [Pubmed]
  6. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Altamirano, M.M., Blackburn, J.M., Aguayo, C., Fersht, A.R. Nature (2000) [Pubmed]
  7. Mutations in TrpI binding site II that differentially affect activation of the trpBA promoter of Pseudomonas aeruginosa. Gao, J., Gussin, G.N. EMBO J. (1991) [Pubmed]
  8. Autogenous regulation of the inducible tryptophan synthase of Pseudomonas putida. Proctor, A.R., Crawford, I.P. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  9. The role of the TRP1 gene in yeast tryptophan biosynthesis. Braus, G.H., Luger, K., Paravicini, G., Schmidheini, T., Kirschner, K., Hütter, R. J. Biol. Chem. (1988) [Pubmed]
  10. Limited proteolysis of N-(5'-phosphoribosyl)anthranilate isomerase: indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domains. Kirschner, K., Szadkowski, H., Henschen, A., Lottspeich, F. J. Mol. Biol. (1980) [Pubmed]
  11. Isolation and characterization of two tryptophan biosynthetic enzymes, indoleglycerol phosphate synthase and phosphoribosyl anthranilate isomerase, from Bacillus subtilis. Hoch, S.O. J. Bacteriol. (1979) [Pubmed]
  12. Photoaffinity labeling of the indole sites on the Escherichia coli tryptophan synthase alpha-subunit. Brock, P.W., Myers, R., Baker, D.C., Hardman, J.K. Arch. Biochem. Biophys. (1983) [Pubmed]
  13. Nucleotide sequence of the Acinetobacter calcoaceticus trpGDC gene cluster. Kaplan, J.B., Goncharoff, P., Seibold, A.M., Nichols, B.P. Mol. Biol. Evol. (1984) [Pubmed]
  14. Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains. Eberhard, M., Tsai-Pflugfelder, M., Bolewska, K., Hommel, U., Kirschner, K. Biochemistry (1995) [Pubmed]
  15. Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes. Stehlin, C., Dahm, A., Kirschner, K. FEBS Lett. (1997) [Pubmed]
  16. Isolation of the DNA sequence coding indole-3-glycerol phosphate synthetase and phosphoribosylanthranilate isomerase of Schizophyllum commune. Muñoz-Rivas, A.M., Specht, C.A., Ullrich, R.C., Novotny, C.P. Curr. Genet. (1986) [Pubmed]
  17. Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (alphaD60N) tryptophan synthase alpha2beta2 complex reveals the correct orientation of active site alphaGlu49. Rhee, S., Miles, E.W., Davies, D.R. J. Biol. Chem. (1998) [Pubmed]
  18. Purification and characterization of the trifunctional beta-subunit of anthranilate synthase from Neurospora crassa. Walker, M.S., DeMoss, J.A. J. Biol. Chem. (1983) [Pubmed]
  19. Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex. Kirschner, K., Lane, A.N., Strasser, A.W. Biochemistry (1991) [Pubmed]
  20. The folding of the bifunctional TRP3 protein in yeast is influenced by a translational pause which lies in a region of structural divergence with Escherichia coli indoleglycerol-phosphate synthase. Crombie, T., Boyle, J.P., Coggins, J.R., Brown, A.J. Eur. J. Biochem. (1994) [Pubmed]
  21. Biosynthesis of sespendole. Uchida, R., Tomoda, H., Omura, S. J. Antibiot. (2006) [Pubmed]
  22. Inactivation and partial degradation of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase in nongrowing cultures of Escherichia coli. Mosteller, R.D., Nishimoto, K.R., Goldstein, R.V. J. Bacteriol. (1977) [Pubmed]
  23. Ordering tryptophan synthase genes of Pseudomonas aeruginosa by cloning in Escherichia coli. Manch, J.N., Crawford, I.P. J. Bacteriol. (1981) [Pubmed]
  24. In vitro determination of the effect of indoleglycerol phosphate on the interaction of purified TrpI protein with its DNA-binding sites. Chang, M., Crawford, I.P. J. Bacteriol. (1991) [Pubmed]
  25. Relative activities and stabilities of mutant Escherichia coli tryptophan synthase alpha subunits. Lim, W.K., Shin, H.J., Milton, D.L., Hardman, J.K. J. Bacteriol. (1991) [Pubmed]
  26. The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product. Hennig, M., Darimont, B.D., Jansonius, J.N., Kirschner, K. J. Mol. Biol. (2002) [Pubmed]
  27. Improving the catalytic activity of a thermophilic enzyme at low temperatures. Merz, A., Yee, M.C., Szadkowski, H., Pappenberger, G., Crameri, A., Stemmer, W.P., Yanofsky, C., Kirschner, K. Biochemistry (2000) [Pubmed]
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