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)
 

Editor

Share

Personal info

View

Links

  • Homologues
  • NCBI Gene
  • NCBI SNP
  • iHOP resource
  • SNPedia

Table of contents

About

Terms

 

Gene Review: 

AOX1  -  aldehyde oxidase 1

Gallus gallus

 
 
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.
 

High impact information on AOX1

  • Rodents are characterized by four aldehyde oxidases as follows: AOX1 and aldehyde oxidase homologs 1-3 (AOH1, AOH2, and AOH3) [1].
  • The avian genome contains two aldehyde oxidase genes, AOX1 and AOH, mapping to chromosome 7 [1].
  • Purification of the chicken AOX1 protein to homogeneity from kidney demonstrates that the enzyme possesses retinaldehyde oxidase activity [1].
  • The average FAD reduction potential is substantially more positive in AO (Em for FAD/FADH., -258 mV; FADH./FADH2, -212 mV at pH 7.8) than in XO or XDH [2].
  • Properties of the prosthetic groups of rabbit liver aldehyde oxidase: a comparison of molybdenum hydroxylase enzymes [2].
 

Associations of AOX1 with chemical compounds

  • Although magnetic interaction between FAD and one or both reduced Fe/S centers has been detected in both AO and XO, no magnetic interaction between the two reduced Fe/S centers themselves was found in AO (although such interaction has been seen in XO) [2].

References

  1. Avian and canine aldehyde oxidases. Novel insights into the biology and evolution of molybdo-flavoenzymes. Terao, M., Kurosaki, M., Barzago, M.M., Varasano, E., Boldetti, A., Bastone, A., Fratelli, M., Garattini, E. J. Biol. Chem. (2006) [Pubmed]
  2. Properties of the prosthetic groups of rabbit liver aldehyde oxidase: a comparison of molybdenum hydroxylase enzymes. Barber, M.J., Coughlan, M.P., Rajagopalan, K.V., Siegel, L.M. Biochemistry (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 WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities