ArticleInternational journal of molecular sciences2020
Exploring the Role of Phenylalanine Residues in Modulating the Flexibility and Topography of the Active Site in the Peroxygenase Variant PaDa-I.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Identification of Key Active-Site Positions Controlling the Chemoselectivity of Aspergillus Brasiliensis Unspecific Peroxygenase.Chembiochem : a European journal of chemical biology · 2025Article
- Recent Progress on Peroxidase Modification and Application.Applied biochemistry and biotechnology · 2024Review
- Hemoprotein Catalyzed Oxygenations: P450s, UPOs, and Progress toward Scalable Reactions.JACS Au · 2021Review
- Ether Oxidation by an Evolved Fungal Heme-Peroxygenase: Insights into Substrate Recognition and Reactivity.Journal of fungi (Basel, Switzerland) · 2021Article
- Identification and Expression of New Unspecific Peroxygenases - Recent Advances, Challenges and Opportunities.Frontiers in bioengineering and biotechnology · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Unspecific peroxygenases (UPOs) are fungal heme-thiolate enzymes able to catalyze a wide range of oxidation reactions, such as peroxidase-like, catalase-like, haloperoxidase-like, and, most interestingly, cytochrome P450-like. One of the most outstanding properties of these enzymes is the ability to catalyze the oxidation a wide range of organic substrates (both aromatic and aliphatic) through cytochrome P450-like reactions (the so-called peroxygenase activity), which involves the insertion of an oxygen atom from hydrogen peroxide. To catalyze this reaction, the substrate must access a channel connecting the bulk solution to the heme group. The composition, shape, and flexibility of this channel surely modulate the catalytic ability of the enzymes in this family. In order to gain an understanding of the role of the residues comprising the channel, mutants derived from PaDa-I, a laboratory-evolved UPO variant from
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Registered trials
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