期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 295, 期 16, 页码 5377-5389出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.REV119.007741
关键词
metalloenzyme; molybdenum; mouse; drug metabolism; flavoprotein; xenobiotic; oxidase; oxygen radicals; iron-sulfur protein; aldehyde oxidase (AOX); enzyme evolution; metal-containing enzyme; molybdenum cofactor (Moco); molybdo-flavoenzyme; 2Fe-2S cluster; flavin adenine dinucleotide (FAD)
资金
- Deutsche Forschungsgemeinschaft [Le1171/8-3]
- FCT-MCTES, research unit UCIBIO [UID/Multi/04378/2019, PTDC/BBB-BEP/1185/2014]
- Fondazione Italo Monzino
- Associazione per la Ricerca sul Cancro (AIRC)
Aldehyde oxidases (AOXs) are a small group of enzymes belonging to the larger family of molybdo-flavoenzymes, along with the well-characterized xanthine oxidoreductase. The two major types of reactions that are catalyzed by AOXs are the hydroxylation of heterocycles and the oxidation of aldehydes to their corresponding carboxylic acids. Different animal species have different complements of AOX genes. The two extremes are represented in humans and rodents; whereas the human genome contains a single active gene (AOX1), those of rodents, such as mice, are endowed with four genes (Aox1-4), clustering on the same chromosome, each encoding a functionally distinct AOX enzyme. It still remains enigmatic why some species have numerous AOX enzymes, whereas others harbor only one functional enzyme. At present, little is known about the physiological relevance of AOX enzymes in humans and their additional forms in other mammals. These enzymes are expressed in the liver and play an important role in the metabolisms of drugs and other xenobiotics. In this review, we discuss the expression, tissue-specific roles, and substrate specificities of the different mammalian AOX enzymes and highlight insights into their physiological roles.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据