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Mammalian aldehyde oxidases: genetics, evolution and biochemistry.
E Garattini1, M Fratelli, M Terao
1Laboratory of Molecular Biology, Istituto di Ricerche Farmacologiche Mario Negri, via La Masa 19, Milan, Italy. egarattini@marionegri.it
Cellular and Molecular Life Sciences : CMLS
|December 11, 2007
Summary
Mammalian aldehyde oxidases, molybdo-flavoenzymes, are crucial for drug metabolism. This review details their genetics, evolution, structure, and tissue distribution in mammals.
Area of Science:
- Biochemistry
- Enzymology
- Genetics
Background:
- Mammalian aldehyde oxidases are molybdo-flavoenzymes involved in hydroxylation and oxidation reactions.
- They play a role in the hepatic metabolism of drugs and toxic compounds.
- Species exhibit varied aldehyde oxidase gene complements, with humans having one and rodents/marsupials having four.
Purpose of the Study:
- To provide a comprehensive overview of mammalian aldehyde oxidases.
- To consolidate current knowledge on their genetics, evolution, structure, and function.
- To highlight their physiological relevance and regulatory mechanisms.
Main Methods:
- Literature review of existing research on mammalian aldehyde oxidases.
- Comparative analysis of gene organization across different species.
- Summary of biochemical and structural data.
Main Results:
- Aldehyde oxidases catalyze heterocyclic hydroxylation and aldehyde oxidation to carboxylic acids.
- Gene duplication events have led to varied gene numbers across species.
- Enzymes are primarily found in the liver and involved in xenobiotic metabolism.
Conclusions:
- Aldehyde oxidases are significant in mammalian physiology, particularly in drug and toxin metabolism.
- Further research is needed to fully elucidate their physiological roles.
- Understanding their genetics and evolution provides insight into species-specific metabolic capabilities.
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