ArticleThe Journal of biological chemistry2012
The first mammalian aldehyde oxidase crystal structure: insights into substrate specificity.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 90 citations in OpenAlex.
- High-resolution structural-omics of human liver enzymes.Cell reports · 2023Article
- Recent advances in the translation of drug metabolism and pharmacokinetics science for drug discovery and development.Acta pharmaceutica Sinica. B · 2022Review
- Association of Mutations Identified in Xanthinuria with the Function and Inhibition Mechanism of Xanthine Oxidoreductase.Biomedicines · 2021Review
- Identification of aldehyde oxidase 3 as a binding protein for squid ink polysaccharides using magnetic nanoparticles.RSC advances · 2021Article
- Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes.The Journal of biological chemistry · 2020Review
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
- Survey of allele specific expression in bovine muscle.Scientific reports · 2019Article
- Fast Methods for Prediction of Aldehyde Oxidase-Mediated Site-of-Metabolism.Computational and structural biotechnology journal · 2019Article
- From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC.Molecules (Basel, Switzerland) · 2018Review
- Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes.Redox biology · 2018Review
- Direct comparison of the four aldehyde oxidase enzymes present in mouse gives insight into their substrate specificities.PloS one · 2018Article
- A eukaryotic nicotinate-inducible gene cluster: convergent evolution in fungi and bacteria.Open biology · 2017Article
- Pyrido[3,4-d]pyrimidin-4(3H)-one metabolism mediated by aldehyde oxidase is blocked by C2-substitution.Xenobiotica; the fate of foreign compounds in biological systems · 2017Article
- Article
- Aldehyde Oxidase 4 Plays a Critical Role in Delaying Silique Senescence by Catalyzing Aldehyde Detoxification.Plant physiology · 2017Article
- Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism.Redox report : communications in free radical research · 2017Review
- Mouse aldehyde-oxidase-4 controls diurnal rhythms, fat deposition and locomotor activity.Scientific reports · 2016Article
- Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase.Nature chemical biology · 2015Article
- Interspecies differences in the metabolism of methotrexate: An insight into the active site differences between human and rabbit aldehyde oxidase.Biochemical pharmacology · 2015Article
- A novel reaction mediated by human aldehyde oxidase: amide hydrolysis of GDC-0834.Drug metabolism and disposition: the biological fate of chemicals · 2015Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAldehyde oxidases have pharmacological relevance, and AOX3 is the major drug-metabolizing enzyme in rodents.
resultsThe crystal structure of mouse AOX3 with kinetics and molecular docking studies provides insights into its enzymatic characteristics.
conclusionDifferences in substrate and inhibitor specificities can be rationalized by comparing the AOX3 and xanthine oxidase structures. SIGNIFICANCE: The first aldehyde oxidase structure represents a major advance for drug design and mechanistic studies. Aldehyde oxidases (AOXs) are homodimeric proteins belonging to the xanthine oxidase family of molybdenum-containing enzymes. Each 150-kDa monomer contains a FAD redox cofactor, two spectroscopically distinct [2Fe-2S] clusters, and a molybdenum cofactor located within the protein active site. AOXs are characterized by broad range substrate specificity, oxidizing different aldehydes and aromatic N-heterocycles. Despite increasing recognition of its role in the metabolism of drugs and xenobiotics, the physiological function of the protein is still largely unknown. We have crystallized and solved the crystal structure of mouse liver aldehyde oxidase 3 to 2.9 Å. This is the first mammalian AOX whose structure has been solved. The structure provides important insights into the protein active center and further evidence on the catalytic differences characterizing AOX and xanthine oxidoreductase. The mouse liver aldehyde oxidase 3 three-dimensional structure combined with kinetic, mutagenesis data, molecular docking, and molecular dynamics studies make a decisive contribution to understand the molecular basis of its rather broad substrate specificity.
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