{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T00:58:49Z","timestamp":1785286729571,"version":"3.55.0"},"reference-count":54,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2024,8,5]],"date-time":"2024-08-05T00:00:00Z","timestamp":1722816000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Bioeng. Biotechnol."],"abstract":"<jats:p><jats:bold>Introduction:<\/jats:bold> Aryl-alcohol oxidase (AAO) shows a pronounced duality as oxidase and dehydrogenase similar to that described for other glucose-methanol-choline (GMC) oxidase\/dehydrogenase superfamily proteins involved in lignocellulose decomposition. In this work, we detail the overall mechanism of AAOs from <jats:italic>Pleurotus eryngii<\/jats:italic> and <jats:italic>Bjerkandera adusta<\/jats:italic> for catalyzing the oxidation of natural aryl-alcohol substrates using either oxygen or quinones as electron acceptors and describe the crystallographic structure of AAO from <jats:italic>B. adusta<\/jats:italic> in complex with a product analogue.<\/jats:p><jats:p><jats:bold>Methods:<\/jats:bold> Kinetic studies with 4-methoxybenzyl and 3-chloro-4- methoxybenzyl alcohols, including both transient-state and steady-state analyses, along with interaction studies, provide insight into the oxidase and dehydrogenase mechanisms of these enzymes. Moreover, the resolution of the crystal structure of AAO from <jats:italic>B. adusta<\/jats:italic> allowed us to compare their overall folding and the structure of the active sites of both AAOs in relation to their activities.<\/jats:p><jats:p><jats:bold>Results and Discussion:<\/jats:bold> Although both enzymes show similar mechanistic properties, notable differences are highlighted in this study. In <jats:italic>B. adusta<\/jats:italic>, the AAO oxidase activity is limited by the reoxidation of the flavin, while in <jats:italic>P. eryngii<\/jats:italic> the slower step takes place during the reductive half-reaction, which determines the overall reaction rate. By contrast, dehydrogenase activity in both enzymes, irrespective of the alcohol participating in the reaction, is limited by the hydroquinone release from the active site. Despite these differences, both AAOs are more efficient as dehydrogenases, supporting the physiological role of this activity in lignocellulosic decay. This dual activity would allow these enzymes to adapt to different environments based on the available electron acceptors.<\/jats:p>","DOI":"10.3389\/fbioe.2024.1440598","type":"journal-article","created":{"date-parts":[[2024,8,5]],"date-time":"2024-08-05T04:54:51Z","timestamp":1722833691000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":6,"title":["Unveiling the kinetic versatility of aryl-alcohol oxidases with different electron acceptors"],"prefix":"10.3389","volume":"12","author":[{"given":"Ana","family":"Serrano","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paula","family":"Cinca-Fernando","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Carro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adri\u00e1n","family":"Vel\u00e1zquez-Campoy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Mart\u00ednez-J\u00falvez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c1ngel T.","family":"Mart\u00ednez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Ferreira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2024,8,5]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"768","DOI":"10.1002\/elsc.201800039","article-title":"Lignocellulose degradation: an overview of fungi and fungal enzymes involved in lignocellulose degradation","volume":"18","author":"Andlar","year":"2018","journal-title":"Eng. 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