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Gene Review

Aox3  -  aldehyde oxidase 3

Mus musculus

Synonyms: 1200011D03Rik, AI326299, AOH1, Aldehyde oxidase 3, Aldehyde oxidase homolog 1, ...
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High impact information on Aox3

  • Rodents are characterized by four aldehyde oxidases as follows: AOX1 and aldehyde oxidase homologs 1-3 (AOH1, AOH2, and AOH3) [1].
  • The enzyme possesses aldehyde oxidase activity and oxidizes, albeit with low efficiency, exogenous substrates that are recognized by AOH1 and AOX1 [2].
  • The AOH3 cDNA is characterized by remarkable similarity to AOX1, AOH1, AOH2, and xanthine oxidoreductase cDNAs [2].
  • However, relative to CD-1 animals, an over 2 log reduction in the steady-state levels of liver AOH1 mRNA, protein, and enzymatic activity is observed in basal conditions and following administration of testosterone [3].
  • The AOH1 and AOH2 genes are 98 and 60 kilobases long, respectively, and consist of 35 coding exons [4].

Biological context of Aox3


Anatomical context of Aox3


Associations of Aox3 with chemical compounds

  • Furthermore, the AOH1 protein has benzaldehyde oxidizing activity with electrophoretic characteristics identical to those of a previously identified aldehyde oxidase isoenzyme (Holmes, R. S. (1979) Biochem. Genet. 17, 517-528) [5].
  • Employing an aldehyde oxidase specific substrate, AOX1/AOH1 activity was shown to be induced by dioxin in mouse liver [6].
  • This activity was inhibited by a known inhibitor of aldehyde oxidases, and eliminated by including tungstate in the mouse diet, which is known to lead to inactivation of molybdoflavoenzymes, thus confirming that the enzymatic activity was attributable to AOX1/AOH1 [6].

Other interactions of Aox3

  • In addition, we have cloned the cDNAs coding for rat AOH1 and AOH2, demonstrating that this animal species has the same complement of molybdo-flavoproteins as the mouse [2].


  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. The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa. Kurosaki, M., Terao, M., Barzago, M.M., Bastone, A., Bernardinello, D., Salmona, M., Garattini, E. J. Biol. Chem. (2004) [Pubmed]
  3. Regulation and biochemistry of mouse molybdo-flavoenzymes. The DBA/2 mouse is selectively deficient in the expression of aldehyde oxidase homologues 1 and 2 and represents a unique source for the purification and characterization of aldehyde oxidase. Vila, R., Kurosaki, M., Barzago, M.M., Kolek, M., Bastone, A., Colombo, L., Salmona, M., Terao, M., Garattini, E. J. Biol. Chem. (2004) [Pubmed]
  4. Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1. Terao, M., Kurosaki, M., Marini, M., Vanoni, M.A., Saltini, G., Bonetto, V., Bastone, A., Federico, C., Saccone, S., Fanelli, R., Salmona, M., Garattini, E. J. Biol. Chem. (2001) [Pubmed]
  5. Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase. Terao, M., Kurosaki, M., Saltini, G., Demontis, S., Marini, M., Salmona, M., Garattini, E. J. Biol. Chem. (2000) [Pubmed]
  6. Identification of aldehyde oxidase 1 and aldehyde oxidase homologue 1 as dioxin-inducible genes. Rivera, S.P., Choi, H.H., Chapman, B., Whitekus, M.J., Terao, M., Garattini, E., Hankinson, O. Toxicology (2005) [Pubmed]
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