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首页> 外文期刊>Archives of Toxicology >Structure and function of mammalian aldehyde oxidases
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Structure and function of mammalian aldehyde oxidases

机译：哺乳动物醛氧化酶的结构和功能

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Mammalian aldehyde oxidases (AOXs; EC1.2.3.1) are a group of conserved proteins belonging to the family of molybdo-flavoenzymes along with the structurally related xanthine dehydrogenase enzyme. AOXs are characterized by broad substrate specificity, oxidizing not only aromatic and aliphatic aldehydes into the corresponding carboxylic acids, but also hydroxylating a series of heteroaromatic rings. The number of AOX isoenzymes expressed in different vertebrate species is variable. The two extremes are represented by humans, which express a single enzyme (AOX1) in many organs and mice or rats which are characterized by tissue-specific expression of four isoforms (AOX1, AOX2, AOX3, and AOX4). In vertebrates each AOX isoenzyme is the product of a distinct gene consisting of 35 highly conserved exons. The extant species-specific complement of AOX isoenzymes is the result of a complex evolutionary process consisting of a first phase characterized by a series of asynchronous gene duplications and a second phase where the pseudogenization and gene deletion events prevail. In the last few years remarkable advances in the elucidation of the structural characteristics and the catalytic mechanisms of mammalian AOXs have been made thanks to the successful crystallization of human AOX1 and mouse AOX3. Much less is known about the physiological function and physiological substrates of human AOX1 and other mammalian AOX isoenzymes, although the importance of these proteins in xenobiotic metabolism is fairly well established and their relevance in drug development is increasing. This review article provides an overview and a discussion of the current knowledge on mammalian AOX.
机译：哺乳动物醛氧化酶（AOXs; EC1.2.3.1）是一组保守的蛋白质，属于钼黄素酶家族，与结构相关的黄嘌呤脱氢酶同在。 AOX的特点是具有广泛的底物特异性，不仅可以将芳族和脂族醛氧化为相应的羧酸，还可以将一系列杂芳环羟基化。在不同脊椎动物物种中表达的AOX同工酶的数量是可变的。这两个极端由人类代表，它们在许多器官和小鼠或大鼠中表达一种酶（AOX1），其特征是四种同工型（AOX1，AOX2，AOX3和AOX4）的组织特异性表达。在脊椎动物中，每种AOX同工酶都是由35个高度保守的外显子组成的独特基因的产物。现有的AOX同工酶物种特异性互补是复杂的进化过程的结果，该过程包括以一系列异步基因重复为特征的第一阶段和伪基因化和基因缺失事件占主导的第二阶段。在过去的几年中，由于人类AOX1和小鼠AOX3的成功结晶，在阐明哺乳动物AOX的结构特征和催化机理方面取得了显着进展。尽管人AOX1和其他哺乳动物AOX同工酶的生理功能和生理底物知之甚少，但这些蛋白在异源生物代谢中的重要性已得到充分确立，并且它们在药物开发中的相关性正在增加。这篇评论文章提供了有关哺乳动物AOX的当前知识的概述和讨论。

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