Structure and function of mammalian aldehyde oxidases
Abstract
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.
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BH4 plays a critical role in the catalytic cycle of NOS.
“In addition, BH4 plays a critical role in the catalytic cycle of NOS (87, 204, 377, 904, 933, 1000, 1007).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [933]
BH4 can be oxidized in vivo by molecular oxygen or ROS to generate dihydrobiopterin (BH2), a pterin unable to support NO synthesis.
“BH4 can be oxidized in vivo by molecular oxygen or ROS to generate dihydrobiopterin (BH2), a pterin very structurally similar to BH4 but unable to support NO synthesis (544, 753, 933).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [933]
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Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
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- Authors
- Terao, M., Romão, M. J., Leimkühler, S., Bolis, M., Fratelli, M., Coelho, C., Santos-Silva, T., & Garattini, E.
- Affiliations
- Mario Negri Institute for Pharmacological Research (IT)
- Universidade Nova de Lisboa (PT)
- University of Potsdam (DE)
- Corresponding author
- Garattini, Enrico
- ORCID
- Venue
- Archives of Toxicology
- Published
- 2016-02-26
- Volume
- 90
- Issue
- 4
- Pages
- 753-780
- ISSN
- 0340-5761 (ISSN-L)
- 1432-0738
- OpenAlex
- W2289764719
- Cited by
- 112
- References
- 151
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 12 · 2023: 7 · 2022: 7 · 2021: 19 · 2020: 11 · 2019: 13 · 2018: 15 · 2017: 12 · 2016: 4
- FWCI
- 2.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Archives of Toxicology (publishedVersion)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- publish.UP (University of Potsdam) (submittedVersion)
- Topics
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- aldehyde oxidase, AOX1, AOX2, xanthine dehydrogenase, enzyme structure, catalytic mechanism, gene duplication, pseudogenization, gene deletion, xenobiotic metabolism, drug development, aldehyde oxidation
- MeSH terms
- Aldehyde Oxidoreductases, Animals, Catalysis, Escherichia coli, Humans, Mammals, Inactivation, Metabolic, Xenobiotics, Crystallography, X-Ray, Evolution, Molecular, Polymorphism, Single Nucleotide, Aldehyde Oxidase
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