The First Mammalian Aldehyde Oxidase Crystal Structure
| Autor: | Catarina Coelho, Mineko Terao, Silke Leimkühler, Martin Mahro, Alexandra T. P. Carvalho, Maria João Romão, José Trincão, Maria J. Ramos, Enrico Garattini |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences biology Stereochemistry Molybdopterin Active site Cell Biology 010402 general chemistry 01 natural sciences Biochemistry Cofactor 0104 chemical sciences 03 medical and health sciences chemistry.chemical_compound Enzyme chemistry Oxidoreductase biology.protein Molybdenum cofactor Xanthine oxidase Molecular Biology Aldehyde oxidase 030304 developmental biology |
| Zdroj: | Journal of Biological Chemistry. 287:40690-40702 |
| ISSN: | 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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