|ZFIN ID: ZDB-PUB-150507-12|
Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression
Kurosaki, M., Bolis, M., Fratelli, M., Barzago, M.M., Pattini, L., Perretta, G., Terao, M., Garattini, E.
|Source:||Cellular and molecular life sciences : CMLS 70(10): 1807–1830 (Journal)|
|Keywords:||Aldehyde oxidase, Molybdo-flavoenzyme, Drug metabolism, Molybdenum cofactor|
|PubMed:||23263164 Full text @ Cell. Mol. Life Sci.|
Kurosaki, M., Bolis, M., Fratelli, M., Barzago, M.M., Pattini, L., Perretta, G., Terao, M., Garattini, E. (2013) Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression. Cellular and molecular life sciences : CMLS. 70(10):1807–1830.
ABSTRACTAldehyde oxidases (AOXs) and xanthine dehydrogenases (XDHs) belong to the family of molybdo-flavoenzymes. Although AOXs are not identifiable in fungi, these enzymes are represented in certain protists and the majority of plants and vertebrates. The physiological functions and substrates of AOXs are unknown. Nevertheless, AOXs are major drug metabolizing enzymes, oxidizing a wide range of aromatic aldehydes and heterocyclic compounds of medical/toxicological importance. Using genome sequencing data, we predict the structures of AOX genes and pseudogenes, reconstructing their evolution. Fishes are the most primitive organisms with an AOX gene (AOXα), originating from the duplication of an ancestral XDH. Further evolution of fishes resulted in the duplication of AOXα into AOXβ and successive pseudogenization of AOXα. AOXβ is maintained in amphibians and it is the likely precursors of reptilian, avian, and mammalian AOX1. Amphibian
- Genes / Markers (2)