Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Gene Review:

aroD - 3-dehydroquinate dehydratase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1691, JW1683

Lamb, H.K. et al., Duncan, K. et al., Chaudhuri, S. et al., Johansson, L. et al., Lalonde, G. et al.

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 aroD

An amended nucleotide sequence for the E. coli gene (aroD) that encode 3-dehydroquinase is also presented, along with a revised alignment of the deduced amino acid sequences for the biosynthetic enzymes [1].

High impact information on aroD

The A. pleuropneumoniae gene, termed aroQ, displays no base or amino acid sequence homology to aroD of E. coli [2].
We have previously reported that the AROM dehydroquinate synthase and 3-dehydroquinate dehydratase are stable and functional as individual domains, but that the 5-enol-pyruvylshikimate-3-phosphate synthase is only active as part of the complete AROM protein or as a bi-domain fragment with dehydroquinate synthase [3].
The genes, ydiB, aroD and ydiN, were strongly induced only in carbon-limited W3110.shik1 [4].

Biological context of aroD

The amino acid sequence was deduced from the nucleotide sequence of the aroD gene and confirmed by determining the amino acid composition of the overproduced enzyme and its N-terminal amino acid sequence [5].

References

Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases. Chaudhuri, S., Duncan, K., Graham, L.D., Coggins, J.R. Biochem. J. (1991) [Pubmed]
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]
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]
Transcriptome analysis of a shikimic acid producing strain of Escherichia coli W3110 grown under carbon- and phosphate-limited conditions. Johansson, L., Lid??n, G. J. Biotechnol. (2006) [Pubmed]
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]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg