Aryl-alcohol oxidases: catalysis, diversity, structure-function and emerging biotechnological applications.

IF 3.9 3区 生物学 Q2 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Paula Cinca-Fernando, Aurora Vázquez-Rodríguez, Juan Mangas-Sánchez, Patricia Ferreira
{"title":"Aryl-alcohol oxidases: catalysis, diversity, structure-function and emerging biotechnological applications.","authors":"Paula Cinca-Fernando, Aurora Vázquez-Rodríguez, Juan Mangas-Sánchez, Patricia Ferreira","doi":"10.1007/s00253-025-13538-7","DOIUrl":null,"url":null,"abstract":"<p><p>Aryl-alcohol oxidases (AAOs) are flavin-dependent enzymes of the glucose-methanol-choline (GMC) oxidoreductase superfamily that catalyze the oxidation of a broad range of activated primary alcohols into their corresponding aldehydes, generating hydrogen peroxide. While traditionally studied in wood-decaying fungi, AAOs have recently been identified in bacteria and arthropods, revealing unexpected structural and functional diversity. These enzymes display broad substrate promiscuity, with preferences shaped by differences in active-site architecture and physicochemical properties. Structural studies across kingdoms show a conserved GMC fold with specific adaptations in substrate-binding domains. Detailed mechanistic insights-particularly from the AAO from Pleurotus eryngii-suggest a consensus hydride transfer mechanism involving conserved histidine residues, enabling both oxidase and dehydrogenase activity. To explore AAO diversity, BLAST-based mining was performed across fungal, bacterial, and arthropod genomes, leading to the identification and classification of hundreds of putative AAO sequences. These have been further grouped into distinct structural and evolutionary types based on conserved motifs and active-site architecture, revealing convergent strategies and potential functional specialization across kingdoms. Beyond their natural role in biomass degradation, AAOs hold significant biotechnological potential in green chemistry, including the synthesis of valuable aldehydes, bioplastics precursors like 2,5-furandicarboxylic acid, and applications in asymmetric synthesis. Recent advances demonstrate the feasibility of integrating AAOs into industrial biocatalytic processes and artificial cascades. This growing understanding of AAO diversity, structure-function relationships, and biotechnological applications paves the way for the development of novel sustainable biocatalysts in chemical, pharmaceutical, and material industries. KEY POINTS: Aryl-alcohol oxidases (AAOs) occur across fungi, bacteria, and arthropods, with distinct structural and functional features. Sequence similarity searches reveal diverse AAO types with distinct structural and evolutionary traits. AAOs enable green synthesis of high-value-added bio-based chemicals.</p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":"151"},"PeriodicalIF":3.9000,"publicationDate":"2025-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12198266/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Microbiology and Biotechnology","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1007/s00253-025-13538-7","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Aryl-alcohol oxidases (AAOs) are flavin-dependent enzymes of the glucose-methanol-choline (GMC) oxidoreductase superfamily that catalyze the oxidation of a broad range of activated primary alcohols into their corresponding aldehydes, generating hydrogen peroxide. While traditionally studied in wood-decaying fungi, AAOs have recently been identified in bacteria and arthropods, revealing unexpected structural and functional diversity. These enzymes display broad substrate promiscuity, with preferences shaped by differences in active-site architecture and physicochemical properties. Structural studies across kingdoms show a conserved GMC fold with specific adaptations in substrate-binding domains. Detailed mechanistic insights-particularly from the AAO from Pleurotus eryngii-suggest a consensus hydride transfer mechanism involving conserved histidine residues, enabling both oxidase and dehydrogenase activity. To explore AAO diversity, BLAST-based mining was performed across fungal, bacterial, and arthropod genomes, leading to the identification and classification of hundreds of putative AAO sequences. These have been further grouped into distinct structural and evolutionary types based on conserved motifs and active-site architecture, revealing convergent strategies and potential functional specialization across kingdoms. Beyond their natural role in biomass degradation, AAOs hold significant biotechnological potential in green chemistry, including the synthesis of valuable aldehydes, bioplastics precursors like 2,5-furandicarboxylic acid, and applications in asymmetric synthesis. Recent advances demonstrate the feasibility of integrating AAOs into industrial biocatalytic processes and artificial cascades. This growing understanding of AAO diversity, structure-function relationships, and biotechnological applications paves the way for the development of novel sustainable biocatalysts in chemical, pharmaceutical, and material industries. KEY POINTS: Aryl-alcohol oxidases (AAOs) occur across fungi, bacteria, and arthropods, with distinct structural and functional features. Sequence similarity searches reveal diverse AAO types with distinct structural and evolutionary traits. AAOs enable green synthesis of high-value-added bio-based chemicals.

芳基醇氧化酶:催化、多样性、结构功能和新兴的生物技术应用。
芳基醇氧化酶(AAOs)是葡萄糖-甲醇-胆碱(GMC)氧化还原酶超家族中的黄素依赖酶,它催化多种活性伯醇氧化成相应的醛,生成过氧化氢。虽然传统上研究木材腐烂真菌,但最近在细菌和节肢动物中发现了AAOs,揭示了意想不到的结构和功能多样性。这些酶表现出广泛的底物混杂性,其偏好由活性位点结构和物理化学性质的差异所决定。跨界的结构研究表明,保守的GMC折叠在底物结合域具有特定的适应性。详细的机制见解-特别是来自杏叶侧边菇的AAO -表明共识的氢化物转移机制涉及保守的组氨酸残基,使氧化酶和脱氢酶都具有活性。为了探索AAO的多样性,我们在真菌、细菌和节肢动物基因组中进行了基于blast的挖掘,从而鉴定和分类了数百个假定的AAO序列。基于保守的基序和活性位点结构,这些被进一步归类为不同的结构和进化类型,揭示了跨王国的收敛策略和潜在的功能专门化。除了在生物质降解中的天然作用外,AAOs在绿色化学中具有重要的生物技术潜力,包括合成有价值的醛,生物塑料前体,如2,5-呋喃二羧酸,以及在不对称合成中的应用。最近的进展证明了将aao整合到工业生物催化过程和人工级联中的可行性。对AAO多样性、结构-功能关系和生物技术应用的日益了解,为化学、制药和材料工业中新型可持续生物催化剂的开发铺平了道路。芳基醇氧化酶(AAOs)存在于真菌、细菌和节肢动物中,具有不同的结构和功能特征。序列相似性搜索显示不同的AAO类型具有不同的结构和进化特征。aao能够实现高附加值生物基化学品的绿色合成。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology 工程技术-生物工程与应用微生物
CiteScore
10.00
自引率
4.00%
发文量
535
审稿时长
2 months
期刊介绍: Applied Microbiology and Biotechnology focusses on prokaryotic or eukaryotic cells, relevant enzymes and proteins; applied genetics and molecular biotechnology; genomics and proteomics; applied microbial and cell physiology; environmental biotechnology; process and products and more. The journal welcomes full-length papers and mini-reviews of new and emerging products, processes and technologies.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信