000144764 001__ 144764
000144764 005__ 20260112133321.0
000144764 0247_ $$2doi$$a10.3389/fbioe.2024.1440598
000144764 0248_ $$2sideral$$a139539
000144764 037__ $$aART-2024-139539
000144764 041__ $$aeng
000144764 100__ $$aSerrano, Ana
000144764 245__ $$aUnveiling the kinetic versatility of aryl-alcohol oxidases with different electron acceptors
000144764 260__ $$c2024
000144764 5060_ $$aAccess copy available to the general public$$fUnrestricted
000144764 5203_ $$aIntroduction: 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 Pleurotus eryngii and Bjerkandera adusta 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 B. adusta in complex with a product analogue. Methods: 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 B. adusta allowed us to compare their overall folding and the structure of the active sites of both AAOs in relation to their activities. Results and Discussion: Although both enzymes show similar mechanistic properties, notable differences are highlighted in this study. In B. adusta, the AAO oxidase activity is limited by the reoxidation of the flavin, while in P. eryngii 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.
000144764 536__ $$9info:eu-repo/grantAgreement/ES/MICINN/PID2022-136369NB-I00$$9info:eu-repo/grantAgreement/EUR/MICINN/TED2021-130803B-I00
000144764 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttps://creativecommons.org/licenses/by/4.0/deed.es
000144764 590__ $$a4.8$$b2024
000144764 592__ $$a0.974$$b2024
000144764 591__ $$aBIOTECHNOLOGY & APPLIED MICROBIOLOGY$$b31 / 177 = 0.175$$c2024$$dQ1$$eT1
000144764 593__ $$aBiomedical Engineering$$c2024$$dQ1
000144764 591__ $$aENGINEERING, BIOMEDICAL$$b35 / 124 = 0.282$$c2024$$dQ2$$eT1
000144764 593__ $$aHistology$$c2024$$dQ1
000144764 593__ $$aBiotechnology$$c2024$$dQ1
000144764 593__ $$aBioengineering$$c2024$$dQ2
000144764 594__ $$a8.8$$b2024
000144764 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000144764 700__ $$aCinca-Fernando, Paula$$uUniversidad de Zaragoza
000144764 700__ $$aCarro, Juan
000144764 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, Adrián$$uUniversidad de Zaragoza
000144764 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, Marta$$uUniversidad de Zaragoza
000144764 700__ $$aMartínez, Ángel T.
000144764 700__ $$0(orcid)0000-0003-4076-6118$$aFerreira, Patricia$$uUniversidad de Zaragoza
000144764 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000144764 773__ $$g12 (2024), 1440598[15 pp.]$$pFront. Bioeng. Biotechnol.$$tFrontiers in Bioengineering and Biotechnology$$x2296-4185
000144764 8564_ $$s3165009$$uhttps://zaguan.unizar.es/record/144764/files/texto_completo.pdf$$yVersión publicada
000144764 8564_ $$s2115173$$uhttps://zaguan.unizar.es/record/144764/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000144764 909CO $$ooai:zaguan.unizar.es:144764$$particulos$$pdriver
000144764 951__ $$a2026-01-12-13:07:01
000144764 980__ $$aARTICLE