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Gene Review

aroD  -  3-dehydroquinate dehydratase

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of aroD

 

High impact information on aroD

  • DNA from these transformants can be recovered by retransformation back into E. coli aroD recipients and selection for chloramphenicol resistance [1].
  • The shikimate pathway enzyme 3-dehydroquinase is very susceptible to inactivation by the group-specific reagent diethyl pyrocarbonate (DEP) [6].
  • These genes code for 3-dehydroquinase enzymes of type II, involved in the catabolism of quinic acid [7].
  • All recombinant cosmids selected for their aroD complementation property carry this sequence [8].
  • No DNA sequence homology has, however, been detected by Southern hybridization between the cloned fragment and the aroD gene of E. coli or the qa2 (catabolic dehydroquinase) gene of Neurospora crassa [8].
 

Chemical compound and disease context of aroD

 

Biological context of aroD

 

Associations of aroD with chemical compounds

  • The presence of shikimic acid in the growth medium restores the ability of an aroD mutant to synthesize cmo5U, while O-succinylbenzoate, which is an early intermediate in the synthesis of menaquinone, does not [15].
  • The addition of an aroD deletion results in a requirement for an aromatic precursor of para-aminobenzoic acid (PABA), an essential bacterial metabolite not present in mammalian tissues [11].
  • The tetracycline-sensitive derivatives of Tn10 mutants obtained were selected on Bochner's medium and checked by DNA-DNA hybridization using aroA and aroD gene specific probes [2].
  • A stable mutation was introduced into the aroD gene of S. typhimurium C5 [4].
  • Additionally we have overproduced and purified the qutB-encoded quinate dehydrogenase and overproduced the qa-2 encoded type II 3-dehydroquinase of Neurospora crassa [16].
 

Other interactions of aroD

 

Analytical, diagnostic and therapeutic context of aroD

References

  1. Chimeric plasmid that replicates autonomously in both Escherichia coli and Neurospora crassa. Hughes, K., Case, M.E., Geever, R., Vapnek, D., Giles, N.H. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  2. Construction of aromatic dependent Shigella flexneri 2a live vaccine candidate strains: deletion mutations in the aroA and the aroD genes. Verma, N.K., Lindberg, A.A. Vaccine (1991) [Pubmed]
  3. Molecular cloning and characterization of the aroD gene encoding 3-dehydroquinase from Salmonella typhi. Servos, S., Chatfield, S., Hone, D., Levine, M., Dimitriadis, G., Pickard, D., Dougan, G., Fairweather, N., Charles, I. J. Gen. Microbiol. (1991) [Pubmed]
  4. Bacteriophage P22 as a vehicle for transducing cosmid gene banks between smooth strains of Salmonella typhimurium: use in identifying a role for aroD in attenuating virulent Salmonella strains. Miller, I.A., Chatfield, S., Dougan, G., Desilva, L., Joysey, H.S., Hormaeche, C. Mol. Gen. Genet. (1989) [Pubmed]
  5. Development of an auxotrophic oral live Shigella flexneri vaccine. Lindberg, A.A., Kärnell, A., Stocker, B.A., Katakura, S., Sweiha, H., Reinholt, F.P. Vaccine (1988) [Pubmed]
  6. Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase. Deka, R.K., Kleanthous, C., Coggins, J.R. J. Biol. Chem. (1992) [Pubmed]
  7. Characterization of a 3-dehydroquinase gene from Actinobacillus pleuropneumoniae with homology to the eukaryotic genes qa-2 and QUTE. Lalonde, G., O'Hanley, P.D., Stocker, B.A., Denich, K.T. Mol. Microbiol. (1994) [Pubmed]
  8. Cloning of a sequence of Aquaspirillum magnetotacticum that complements the aroD gene of Escherichia coli. Berson, A.E., Hudson, D.V., Waleh, N.S. Mol. Microbiol. (1991) [Pubmed]
  9. Construction of an auxotrophic Shigella flexneri strain for use as a live vaccine. Lindberg, A.A., Karnell, A., Pál, T., Sweiha, H., Hultenby, K., Stocker, B.A. Microb. Pathog. (1990) [Pubmed]
  10. Control of metabolic flux through the quinate pathway in Aspergillus nidulans. Wheeler, K.A., Lamb, H.K., Hawkins, A.R. Biochem. J. (1996) [Pubmed]
  11. Genotypic and phenotypic characterization of an aroD deletion-attenuated Escherichia coli K12-Shigella flexneri hybrid vaccine expressing S. flexneri 2a somatic antigen. Newland, J.W., Hale, T.L., Formal, S.B. Vaccine (1992) [Pubmed]
  12. Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. Foster, S.J. J. Gen. Microbiol. (1991) [Pubmed]
  13. The cloning and analysis of the aroD gene of E. coli K-12. Kinghorn, J.R., Schweizer, M., Giles, N.H., Kushner, S.R. Gene (1981) [Pubmed]
  14. The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase. Duncan, K., Chaudhuri, S., Campbell, M.S., Coggins, J.R. Biochem. J. (1986) [Pubmed]
  15. Chorismic acid, a key metabolite in modification of tRNA. Hagervall, T.G., Jönsson, Y.H., Edmonds, C.G., McCloskey, J.A., Björk, G.R. J. Bacteriol. (1990) [Pubmed]
  16. Characterization of the 3-dehydroquinase domain of the pentafunctional AROM protein, and the quinate dehydrogenase from Aspergillus nidulans, and the overproduction of the type II 3-dehydroquinase from neurospora crassa. Hawkins, A.R., Moore, J.D., Adeokun, A.M. Biochem. J. (1993) [Pubmed]
  17. The complex Arom locus of Aspergillus nidulans. Evidence for multiple gene fusions and convergent evolution. Hawkins, A.R. Curr. Genet. (1987) [Pubmed]
  18. Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori. Bottomley, J.R., Clayton, C.L., Chalk, P.A., Kleanthous, C. Biochem. J. (1996) [Pubmed]
  19. Crystallization of a type I 3-dehydroquinase from Salmonella typhi. Boys, C.W., Bury, S.M., Sawyer, L., Moore, J.D., Charles, I.G., Hawkins, A.R., Deka, R., Kleanthous, C., Coggins, J.R. J. Mol. Biol. (1992) [Pubmed]
 
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