ArticleInternational journal of molecular sciences2019
Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed.
- Biocatalytic Arene Functionalization Using Integrated Unspecific Peroxygenase and Halohydrin Dehalogenase.Chem & bio engineering · 2026Article
- Enzyme Co-Immobilization on Precipitated Silica for Sustainable Lactobionic Acid Production.Molecules (Basel, Switzerland) · 2026Article
- Peroxide-Mediated Oxygenation of Organic Compounds by Fungal Peroxygenases.Antioxidants (Basel, Switzerland) · 2022Review
- Enzyme-catalyzed allylic oxidation reactions: A mini-review.Frontiers in chemistry · 2022Review
- A holistic carrier-bound immobilization approach for unspecific peroxygenase.Frontiers in chemistry · 2022Article
- Recent developments in the use of peroxygenases - Exploring their high potential in selective oxyfunctionalisations.Biotechnology advances · 2021Review
- Functional Expression of Two Unusual Acidic Peroxygenases fromApplied and environmental microbiology · 2021Article
- An alginate-confined peroxygenase-CLEA for styrene epoxidation.Chemical communications (Cambridge, England) · 2021Article
- Identification and Expression of New Unspecific Peroxygenases - Recent Advances, Challenges and Opportunities.Frontiers in bioengineering and biotechnology · 2021Review
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Unspecific peroxygenases (UPOs) are highly promiscuous biocatalyst with self-sufficient mono(per)oxygenase activity. A laboratory-evolved UPO secreted by yeast was covalently immobilized in activated carriers through one-point attachment. In order to maintain the desired orientation without compromising the enzyme's activity, the S221C mutation was introduced at the surface of the enzyme, enabling a single disulfide bridge to be established between the support and the protein. Fluorescence confocal microscopy demonstrated the homogeneous distribution of the enzyme, regardless of the chemical nature of the carrier. This immobilized biocatalyst was characterized biochemically opening an exciting avenue for research into applied synthetic chemistry.
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Registered trials
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