ArticleThe Journal of biological chemistry2011
Modulating O2 reactivity in a fungal flavoenzyme: involvement of aryl-alcohol oxidase Phe-501 contiguous to catalytic histidine.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Aryl-alcohol oxidases: catalysis, diversity, structure-function and emerging biotechnological applications.Applied microbiology and biotechnology · 2025Review
- Substrate specificity mapping of fungal CAZy AA3_2 oxidoreductases.Biotechnology for biofuels and bioproducts · 2024Article
- Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme.Nature chemical biology · 2023Article
- Expanding the Physiological Role of Aryl-Alcohol Flavooxidases as Quinone Reductases.Applied and environmental microbiology · 2023Article
- Structure of lactate oxidase from Enterococcus hirae revealed new aspects of active site loop function: Product-inhibition mechanism and oxygen gatekeeper.Protein science : a publication of the Protein Society · 2022Article
- 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
- Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production.Applied and environmental microbiology · 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
- Biocatalytic Enantioselective Oxidation ofAdvanced synthesis & catalysis · 2019Article
- Multiple implications of an active site phenylalanine in the catalysis of aryl-alcohol oxidase.Scientific reports · 2018Article
- Activities of Secreted Aryl Alcohol Quinone Oxidoreductases from Pycnoporus cinnabarinus Provide Insights into Fungal Degradation of Plant Biomass.Applied and environmental microbiology · 2016Article
- Focused Directed Evolution of Aryl-Alcohol Oxidase in Saccharomyces cerevisiae by Using Chimeric Signal Peptides.Applied and environmental microbiology · 2015Article
- The substrate tolerance of alcohol oxidases.Applied microbiology and biotechnology · 2015Review
- Steroid hydroxylation by basidiomycete peroxygenases: a combined experimental and computational study.Applied and environmental microbiology · 2015Article
- Molecular characterization and expression of a novel alcohol oxidase from Aspergillus terreus MTCC6324.PloS one · 2014Article
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Authors and funding
6 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aryl-alcohol oxidase (AAO) is a flavoenzyme responsible for activation of O(2) to H(2)O(2) in fungal degradation of lignin. The AAO crystal structure shows a buried active site connected to the solvent by a hydrophobic funnel-shaped channel, with Phe-501 and two other aromatic residues forming a narrow bottleneck that prevents the direct access of alcohol substrates. However, ligand diffusion simulations show O(2) access to the active site following this channel. Site-directed mutagenesis of Phe-501 yielded a F501A variant with strongly reduced O(2) reactivity. However, a variant with increased reactivity, as shown by kinetic constants and steady-state oxidation degree, was obtained by substitution of Phe-501 with tryptophan. The high oxygen catalytic efficiency of F501W, ∼2-fold that of native AAO and ∼120-fold that of F501A, seems related to a higher O(2) availability because the turnover number was slightly decreased with respect to the native enzyme. Free diffusion simulations of O(2) inside the active-site cavity of AAO (and several in silico Phe-501 variants) yielded >60% O(2) population at 3-4 Å from flavin C4a in F501W compared with 44% in AAO and only 14% in F501A. Paradoxically, the O(2) reactivity of AAO decreased when the access channel was enlarged and increased when it was constricted by introducing a tryptophan residue. This is because the side chain of Phe-501, contiguous to the catalytic histidine (His-502 in AAO), helps to position O(2) at an adequate distance from flavin C4a (and His-502 Nε). Phe-501 substitution with a bulkier tryptophan residue resulted in an increase in the O(2) reactivity of this flavoenzyme.
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