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)
Chemical Compound Review

AGN-PC-004CJI     1,3,4-trihydroxy-5-oxo- cyclohexane-1...

Synonyms: CHEMBL1160497, KST-1A9752, AC1Q6DJO, CTK8D7715, AR-1B6188, ...
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 DEHYDROQUINATE


High impact information on DEHYDROQUINATE


Chemical compound and disease context of DEHYDROQUINATE


Biological context of DEHYDROQUINATE


Associations of DEHYDROQUINATE with other chemical compounds


Gene context of DEHYDROQUINATE


Analytical, diagnostic and therapeutic context of DEHYDROQUINATE

  • Extensive crystallization trials of Aspergillus nidulans dehydroquinate synthase, a potential novel target for antimicrobial drugs, in complexes with different ligands have resulted in the identification of nine crystal forms [16].


  1. Isotope effects in 3-dehydroquinate synthase and dehydratase. Mechanistic implications. Rotenberg, S.L., Sprinson, D.B. J. Biol. Chem. (1978) [Pubmed]
  2. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Bender, S.L., Mehdi, S., Knowles, J.R. Biochemistry (1989) [Pubmed]
  3. Cloning, expression, and characterization of a type II 3-dehydroquinate dehydratase gene from Streptomyces hygroscopicus. Florova, G., Denoya, C.D., Morgenstern, M.R., Skinner, D.D., Reynolds, K.A. Arch. Biochem. Biophys. (1998) [Pubmed]
  4. Salmonella typhimurium aroB mutants are attentuated in BALB/c mice. Günel-Ozcan, A., Brown, K.A., Allen, A.G., Maskell, D.J. Microb. Pathog. (1997) [Pubmed]
  5. Cloning and analysis of the aroB gene encoding dehydroquinate synthase from Corynebacterium glutamicum. Han, M.A., Lee, H.S., Cheon, C.I., Min, K.H., Lee, M.S. Can. J. Microbiol. (1999) [Pubmed]
  6. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Carpenter, E.P., Hawkins, A.R., Frost, J.W., Brown, K.A. Nature (1998) [Pubmed]
  7. Structure of Arabidopsis dehydroquinate dehydratase-shikimate dehydrogenase and implications for metabolic channeling in the shikimate pathway. Singh, S.A., Christendat, D. Biochemistry (2006) [Pubmed]
  8. Comparative analysis of the QUTR transcription repressor protein and the three C-terminal domains of the pentafunctional AROM enzyme. Lamb, H.K., Moore, J.D., Lakey, J.H., Levett, L.J., Wheeler, K.A., Lago, H., Coggins, J.R., Hawkins, A.R. Biochem. J. (1996) [Pubmed]
  9. Efficient independent activity of a monomeric, monofunctional dehydroquinate synthase derived from the N-terminus of the pentafunctional AROM protein of Aspergillus nidulans. Moore, J.D., Coggins, J.R., Virden, R., Hawkins, A.R. Biochem. J. (1994) [Pubmed]
  10. The Mycobacterium tuberculosis shikimate pathway genes: evolutionary relationship between biosynthetic and catabolic 3-dehydroquinases. Garbe, T., Servos, S., Hawkins, A., Dimitriadis, G., Young, D., Dougan, G., Charles, I. Mol. Gen. Genet. (1991) [Pubmed]
  11. Inhibitors of types I and II dehydroquinase. Le Sann, C., Gower, M.A., Abell, A.D. Mini reviews in medicinal chemistry. (2004) [Pubmed]
  12. Active site labeling of the shikimate pathway enzyme, dehydroquinase. Evidence for a common substrate binding site within dehydroquinase and dehydroquinate synthase. Kleanthous, C., Campbell, D.G., Coggins, J.R. J. Biol. Chem. (1990) [Pubmed]
  13. Role of glutamate 243 in the active site of 2-deoxy-scyllo-inosose synthase from Bacillus circulans. Hirayama, T., Kudo, F., Huang, Z., Eguchi, T. Bioorg. Med. Chem. (2007) [Pubmed]
  14. Molecular cloning of the gene for the key carbocycle-forming enzyme in the biosynthesis of 2-deoxystreptamine-containing aminocyclitol antibiotics and its comparison with dehydroquinate synthase. Kudo, F., Tamegai, H., Fujiwara, T., Tagami, U., Hirayama, K., Kakinuma, K. J. Antibiot. (1999) [Pubmed]
  15. Overproduction in Escherichia coli of the dehydroquinate synthase domain of the Aspergillus nidulans pentafunctional AROM protein. van den Hombergh, J.P., Moore, J.D., Charles, I.G., Hawkins, A.R. Biochem. J. (1992) [Pubmed]
  16. Identification of many crystal forms of Aspergillus nidulans dehydroquinate synthase. Nichols, C.E., Ren , J., Lamb, H., Haldane, F., Hawkins, A.R., Stammers, D.K. Acta Crystallogr. D Biol. Crystallogr. (2001) [Pubmed]
WikiGenes - Universities