ArticleScientific reports2018
Multiple implications of an active site phenylalanine in the catalysis of aryl-alcohol oxidase.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Aryl-alcohol oxidases: catalysis, diversity, structure-function and emerging biotechnological applications.Applied microbiology and biotechnology · 2025Review
- Discovery, characterization, and synthetic potential of two novel bacterial aryl-alcohol oxidases.Applied microbiology and biotechnology · 2024Article
- Unveiling the kinetic versatility of aryl-alcohol oxidases with different electron acceptors.Frontiers in bioengineering and biotechnology · 2024Article
- Outer coordination sphere influences on cofactor maturation and substrate oxidation by cytochrome P460.Chemical science · 2023Article
- Expanding the Physiological Role of Aryl-Alcohol Flavooxidases as Quinone Reductases.Applied and environmental microbiology · 2023Article
- Oxidation of 5-hydroxymethylfurfural with a novel aryl alcohol oxidase from Mycobacterium sp. MS1601.Microbial biotechnology · 2022Article
- Pecularities and applications of aryl-alcohol oxidases from fungi.Applied microbiology and biotechnology · 2021Review
- Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production.Nature communications · 2021Article
- TargetingBiology · 2020Article
- Alteration of Electron Acceptor Preferences in the Oxidative Half-Reaction of Flavin-Dependent Oxidases and Dehydrogenases.International journal of molecular sciences · 2020Review
- Directed evolution of the aryl-alcohol oxidase: Beyond the lab bench.Computational and structural biotechnology journal · 2020Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aryl-alcohol oxidase (AAO) has demonstrated to be an enzyme with a bright future ahead due to its biotechnological potential in deracemisation of chiral compounds, production of bioplastic precursors and other reactions of interest. Expanding our understanding on the AAO reaction mechanisms, through the investigation of its structure-function relationships, is crucial for its exploitation as an industrial biocatalyst. In this regard, previous computational studies suggested an active role for AAO Phe397 at the active-site entrance. This residue is located in a loop that partially covers the access to the cofactor forming a bottleneck together with two other aromatic residues. Kinetic and affinity spectroscopic studies, complemented with computational simulations using the recently developed adaptive-PELE technology, reveal that the Phe397 residue is important for product release and to help the substrates attain a catalytically relevant position within the active-site cavity. Moreover, removal of aromaticity at the 397 position impairs the oxygen-reduction activity of the enzyme. Experimental and computational findings agree very well in the timing of product release from AAO, and the simulations help to understand the experimental results. This highlights the potential of adaptive-PELE to provide answers to the questions raised by the empirical results in the study of enzyme mechanisms.
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Registered trials
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