8BB8
Crystal structure of human aldehyde dehydrogenase ALDH3A1 in complex with octanal
8BB8 の概要
| エントリーDOI | 10.2210/pdb8bb8/pdb |
| 分子名称 | Aldehyde dehydrogenase, dimeric NADP-preferring, POTASSIUM ION, ACETATE ION, ... (6 entities in total) |
| 機能のキーワード | aldehyde dehydrogenase, aldh3a1, odorant, oxidoreductase |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 104801.89 |
| 構造登録者 | |
| 主引用文献 | Boichot, V.,Menetrier, F.,Saliou, J.M.,Lirussi, F.,Canon, F.,Folia, M.,Heydel, J.M.,Hummel, T.,Menzel, S.,Steinke, M.,Hackenberg, S.,Schwartz, M.,Neiers, F. Characterization of human oxidoreductases involved in aldehyde odorant metabolism. Sci Rep, 13:4876-4876, 2023 Cited by PubMed Abstract: Oxidoreductases are major enzymes of xenobiotic metabolism. Consequently, they are essential in the chemoprotection of the human body. Many xenobiotic metabolism enzymes have been shown to be involved in chemosensory tissue protection. Among them, some were additionally shown to be involved in chemosensory perception, acting in signal termination as well as in the generation of metabolites that change the activation pattern of chemosensory receptors. Oxidoreductases, especially aldehyde dehydrogenases and aldo-keto reductases, are the first barrier against aldehyde compounds, which include numerous odorants. Using a mass spectrometry approach, we characterized the most highly expressed members of these families in the human nasal mucus sampled in the olfactory vicinity. Their expression was also demonstrated using immunohistochemistry in human epitheliums sampled in the olfactory vicinity. Recombinant enzymes corresponding to three highly expressed human oxidoreductases (ALDH1A1, ALDH3A1, AKR1B10) were used to demonstrate the high enzymatic activity of these enzymes toward aldehyde odorants. The structure‒function relationship set based on the enzymatic parameters characterization of a series of aldehyde odorant compounds was supported by the X-ray structure resolution of human ALDH3A1 in complex with octanal. PubMed: 36966166DOI: 10.1038/s41598-023-31769-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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