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:

gcd - glucose dehydrogenase

Pseudomonas aeruginosa PAO1

Whiting, P.H. et al., Williams, S.G. et al., Mitchell, C.G. et al., Duine, J.A. et al., Hunt, J.C. 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 gcd

A procedure is described for the easy preparation of an apoenzyme from the quinoprotein glucose dehydrogenase of Pseudomonas aeruginosa strains [1].

High impact information on gcd

Such mutants showed no repression of the glucose-transport system by high inflowing concentrations, but with a mutant apparently defective only in glucose dehydrogenase, the addition of gluconate caused repression of the glucose-transport system [2].
4. In the presence of 30mM-citrate and various concentrations of added glucose and gluconate, the activity of the glucose-transport system accorded with the proposal that a major factor concerned in the repression of this system was the concentration of gluconate, produced extracellularly by glucose dehydrogenase [2].
These changes were accompanied by similar decreases in the activities of the alginate biosynthetic enzymes (represented by phosphomannomutase and GDP-mannose dehydrogenase) and by a large increase in the activity of the first enzyme of the 'external' non-phosphorylative pathway of glucose metabolism, glucose dehydrogenase [3].
Failure of Pseudomonas aeruginosa to form membrane-associated glucose dehydrogenase activity during anaerobic growth with nitrate [4].
This change was a consequence of decreased activities of glucose dehydrogenase and gluconate dehydrogenase and of the transport systems for gluconate and 2-oxogluconate, and an increased activity of glucose transport, while relatively high activities of hexokinase and glucose-6-phosphate dehydrogenase were maintained [5].

References

Detection and determination of pyrroloquinoline quinone, the coenzyme of quinoproteins. Duine, J.A., Frank, J., Jongejan, J.A. Anal. Biochem. (1983) [Pubmed]
The regulation of transport of glucose, gluconate and 2-oxogluconate and of glucose catabolism in Pseudomonas aeruginosa. Whiting, P.H., Midgley, M., Dawes, E.A. Biochem. J. (1976) [Pubmed]
Physiological and biochemical changes accompanying the loss of mucoidy by Pseudomonas aeruginosa. Williams, S.G., Greenwood, J.A., Jones, C.W. Microbiology (Reading, Engl.) (1996) [Pubmed]
Failure of Pseudomonas aeruginosa to form membrane-associated glucose dehydrogenase activity during anaerobic growth with nitrate. Hunt, J.C., Phibbs, P.V. Biochem. Biophys. Res. Commun. (1981) [Pubmed]
The role of oxygen in the regulation of glucose metabolism, transport and the tricarboxylic acid cycle in Pseudomonas aeruginosa. Mitchell, C.G., Dawes, E.A. J. Gen. Microbiol. (1982) [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

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.