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Gene Review

aroM  -  hypothetical protein

Escherichia coli CFT073

 
 
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Disease relevance of aroM

 

High impact information on aroM

 

Chemical compound and disease context of aroM

 

Biological context of aroM

 

Associations of aroM with chemical compounds

References

  1. 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]
  2. Inducible overproduction of the Aspergillus nidulans pentafunctional AROM protein and the type-I and -II 3-dehydroquinases from Salmonella typhi and Mycobacterium tuberculosis. Moore, J.D., Lamb, H.K., Garbe, T., Servos, S., Dougan, G., Charles, I.G., Hawkins, A.R. Biochem. J. (1992) [Pubmed]
  3. 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]
  4. 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]
  5. 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]
  6. Overproduction of, and interaction within, bifunctional domains from the amino- and carboxy-termini of the pentafunctional AROM protein of Aspergillus nidulans. Moore, J.D., Hawkins, A.R. Mol. Gen. Genet. (1993) [Pubmed]
 
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