The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

ARO7  -  chorismate mutase ARO7

Saccharomyces cerevisiae S288c

Synonyms: CM, Chorismate mutase, HGS1, OSM2, TYR7, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ARO7


High impact information on ARO7


Chemical compound and disease context of ARO7


Biological context of ARO7

  • The binding sites have been analyzed in the active enzyme by site directed mutagenesis of critical codons of the coding gene, ARO7 [8].
  • The gene we termed YMC1 (yeast mitochondrial carrier) is located on chromosome XVI, closely downstream of ARO7 encoding chorismate mutase [9].
  • Therefore, the evolution of the sophisticated allosteric regulation of yeast chorismate mutase requires as prerequisite (i) that the encoding ARO7 gene is not transcriptionally regulated, whereas (ii) the transcription of the competing feedback-regulated anthranilate synthase-encoding gene is controlled by availability of amino acids [10].
  • The Nal-sensitive aro7 mutant cells were used to show that the resumption of Nal-inhibited nuclear activity and cell proliferation takes place while cytoplasmic Nal persists at concentrations inhibitory for the mutant chorismate mutase [11].
  • The recessive allele of the HGS1 locus, hgs1-1, and the codominant allele of the HGS2 locus, HGS2-1, were necessary for the sensitive phenotypes, and alleles in the MSM1 locus, MSM1-1 and msm1-2, were responsible for the different sensitivity levels [12].

Anatomical context of ARO7

  • As yeast-derived 1F7(Fab) catalyzes the chorismate mutase reaction with the same specific activity as antibody isolated from the hybridoma, our expression system now makes possible the application of classical and "reverse" genetics to the study and improvement of this first-generation abzyme [13].

Associations of ARO7 with chemical compounds

  • Expression of an allosterically unregulated, constitutively activated chorismate mutase encoded by the ARO7(T226I) (ARO7(c)) allele depleted the chorismate pool [10].
  • The crystal structure of the tyrosine-bound T state of allosteric yeast Saccharomyces cerevisiae chorismate mutase was solved by molecular replacement at a resolution of 2.8 angstroms using a monomer of the R-state structure as the search model [14].
  • Yeast chorismate mutase (EC shows homotropic activation by the substrate, allosteric activation by tryptophan, and allosteric inhibition by tyrosine [15].
  • A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions [2].
  • Replacement of Glu-246 in the yeast chorismate mutase by glutamine changes the pH optimum for activity of the enzyme from a narrow to a broad pH range [2].

Other interactions of ARO7

  • Finally, ROX1 was mapped to yeast chromosome XVI, near the ARO7-OSM2 locus [16].
  • A GCN4 protein recognition element is not sufficient for GCN4-dependent regulation of transcription in the ARO7 promoter of Saccharomyces cerevisiae [17].
  • Genetic analyses of the parents and the progeny indicated that the levels of inorganic mercury sensitivity were determined by three distinct loci, HGS1, HGS2 and MSM1 [12].

Analytical, diagnostic and therapeutic context of ARO7


  1. The crystal structure of allosteric chorismate mutase at 2.2-A resolution. Xue, Y., Lipscomb, W.N., Graf, R., Schnappauf, G., Braus, G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  2. A glutamate residue in the catalytic center of the yeast chorismate mutase restricts enzyme activity to acidic conditions. Schnappauf, G., Sträter, N., Lipscomb, W.N., Braus, G.H. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  3. Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Helmstaedt, K., Krappmann, S., Braus, G.H. Microbiol. Mol. Biol. Rev. (2001) [Pubmed]
  4. Refined molecular hinge between allosteric and catalytic domain determines allosteric regulation and stability of fungal chorismate mutase. Helmstaedt, K., Heinrich, G., Lipscomb, W.N., Braus, G.H. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  5. Substrate conformational transitions in the active site of chorismate mutase: their role in the catalytic mechanism. Guo, H., Cui, Q., Lipscomb, W.N., Karplus, M. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  6. Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. Sträter, N., Schnappauf, G., Braus, G., Lipscomb, W.N. Structure (1997) [Pubmed]
  7. Monofunctional chorismate mutase from Bacillus subtilis: FTIR studies and the mechanism of action of the enzyme. Gray, J.V., Knowles, J.R. Biochemistry (1994) [Pubmed]
  8. Tyrosine and tryptophan act through the same binding site at the dimer interface of yeast chorismate mutase. Schnappauf, G., Krappmann, S., Braus, G.H. J. Biol. Chem. (1998) [Pubmed]
  9. YMC1, a yeast gene encoding a new putative mitochondrial carrier protein. Graf, R., Baum, B., Braus, G.H. Yeast (1993) [Pubmed]
  10. Coevolution of transcriptional and allosteric regulation at the chorismate metabolic branch point of Saccharomyces cerevisiae. Krappmann, S., Lipscomb, W.N., Braus, G.H. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  11. Mutations sensitizing yeast cells to the start inhibitor nalidixic acid. Prendergast, J.A., Singer, R.A., Rowley, N., Rowley, A., Johnston, G.C., Danos, M., Kennedy, B., Gaber, R.F. Yeast (1995) [Pubmed]
  12. Saccharomyces cerevisiae strains sensitive to inorganic mercury. I. Effect of tyrosine. Ono, B., Sakamoto, E. Curr. Genet. (1985) [Pubmed]
  13. Yeast expression of a catalytic antibody with chorismate mutase activity. Bowdish, K., Tang, Y., Hicks, J.B., Hilvert, D. J. Biol. Chem. (1991) [Pubmed]
  14. Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state. Strater, N., Hakansson, K., Schnappauf, G., Braus, G., Lipscomb, W.N. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  15. Separation of inhibition and activation of the allosteric yeast chorismate mutase. Schnappauf, G., Lipscomb, W.N., Braus, G.H. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  16. The Rox1 repressor of the Saccharomyces cerevisiae hypoxic genes is a specific DNA-binding protein with a high-mobility-group motif. Balasubramanian, B., Lowry, C.V., Zitomer, R.S. Mol. Cell. Biol. (1993) [Pubmed]
  17. A GCN4 protein recognition element is not sufficient for GCN4-dependent regulation of transcription in the ARO7 promoter of Saccharomyces cerevisiae. Schmidheini, T., Mösch, H.U., Graf, R., Braus, G.H. Mol. Gen. Genet. (1990) [Pubmed]
  18. The aroC gene of Aspergillus nidulans codes for a monofunctional, allosterically regulated chorismate mutase. Krappmann, S., Helmstaedt, K., Gerstberger, T., Eckert, S., Hoffmann, B., Hoppert, M., Schnappauf, G., Braus, G.H. J. Biol. Chem. (1999) [Pubmed]
  19. The crystallization and preliminary X-ray analysis of allosteric chorismate mutase. Xue, Y., Lipscomb, W.N. J. Mol. Biol. (1994) [Pubmed]
  20. Cloning and expression in yeast of a higher plant chorismate mutase. Molecular cloning, sequencing of the cDNA and characterization of the Arabidopsis thaliana enzyme expressed in yeast. Eberhard, J., Raesecke, H.R., Schmid, J., Amrhein, N. FEBS Lett. (1993) [Pubmed]
WikiGenes - Universities