9AVH

Crystal structure of an aryl-alcohol-oxidase from Bjerkandera adusta.

9AVH の概要

• エントリーDOI: 10.2210/pdb9avh/pdb
• 分子名称: Aryl Alcohol Oxidase, FLAVIN-ADENINE DINUCLEOTIDE, 4-METHOXYBENZOIC ACID, ... (6 entities in total)
• 機能のキーワード: aao, bjerkandera adusta, oxidoreductase, flavoprotein
• 由来する生物種: Bjerkandera adusta
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64783.13

構造登録者

Martinez-Julvez, M.,Ferreira, P. (登録日: 2024-03-03, 公開日: 2025-01-22)

主引用文献

Serrano, A.,Cinca-Fernando, P.,Carro, J.,Velazquez-Campoy, A.,Martinez-Julvez, M.,Martinez, A.T.,Ferreira, P.
Unveiling the kinetic versatility of aryl-alcohol oxidases with different electron acceptors.
Front Bioeng Biotechnol, 12:1440598-1440598, 2024

PubMed Abstract: 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 and 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 in complex with a product analogue. 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 allowed us to compare their overall folding and the structure of the active sites of both AAOs in relation to their activities. Although both enzymes show similar mechanistic properties, notable differences are highlighted in this study. In , the AAO oxidase activity is limited by the reoxidation of the flavin, while in 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.

PubMed: 39161354
DOI: 10.3389/fbioe.2024.1440598

実験手法

X-RAY DIFFRACTION (1.8 Å)