Discovering Diverse Roles of Peroxidases and Catalases in Photosynthetic and Non-Photosynthetic Eukaryotes

Zámocký, Marcel

doi:10.3390/antiox11122337

Antioxidants

2022

DOI: 10.3390/antiox11122337

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Discovering Diverse Roles of Peroxidases and Catalases in Photosynthetic and Non-Photosynthetic Eukaryotes

Marcel Zámocký

Abstract: This Special Issue of Antioxidants, dedicated to “The Role of Peroxidases and Catalases in Photosynthetic and Non-photosynthetic Eukaryotes“, was accomplished with the contribution of five original research articles and two detailed reviews. [...]

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2024

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In silico analysis of a heme-thiolate peroxidase gene discovered in an ectomycorrhizal fungus of Carpathian primeval forest: implications for biotechnological applications

Kubala,

Ferianc,

Chovanová

et al. 2024

Biologia

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In this work, we focus on the identification of novel fungal peroxygenase gene belonging to the peroxidase-peroxygenase superfamily. We applied a metagenomic approach on soil samples from primeval forest and appropriate bioinformatics tools for analysis of obtained genomic DNA sequence. Peroxidases are ubiquitous metalloenzymes that are able to reduce reactive peroxides, mainly hydrogen peroxide, into water, whereas several substrates can be concomitantly oxidized during their catalytic reaction. Our purpose was to collect unique peroxygenase sequence data originating from a preserved biotope for a robust phylogenetic reconstruction of a particular gene family coding for highly versatile heme-thiolate peroxidases that has peculiar yet undiscovered representatives among ectomycorrhizal fungi. We identified unique DNA sequence, 812 bp long, from ectomycorrhizal Suillus species coding for a heme-thiolate peroxidase with 1 typical intron that appears distinctive for Carpathian forests. After translation in corresponding protein sequence 251 amino acids long we could identify typical signatures of this peroxygenase. On the proximal side of heme we found the conserved P-C-P triad responsible for efficient ligation of heme iron thus influencing the reactivity of this peroxidase. On the distal side we recognized the E-H-D-X-S-L motif for interaction with a stabilizing magnesium ion. Maximum likelihood reconstruction of protein phylogeny revealed with a high bootstrap support the presence of a monophyletic HTP4 clade originating in numerous Suillus representatives. Together with sister clades of edible Boletus and poisonous Paxillus containing diverse peroxygenases these newly discovered heme catalyst can be considered for application of oxyfunctionalization of organic molecules.

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In silico analysis of a heme-thiolate peroxidase gene discovered in an ectomycorrhizal fungus of Carpathian primeval forest: implications for biotechnological applications

Kubala,

Ferianc,

Chovanová

et al. 2024

Biologia

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Discovering Diverse Roles of Peroxidases and Catalases in Photosynthetic and Non-Photosynthetic Eukaryotes

Abstract: This Special Issue of Antioxidants, dedicated to “The Role of Peroxidases and Catalases in Photosynthetic and Non-photosynthetic Eukaryotes“, was accomplished with the contribution of five original research articles and two detailed reviews. [...]

Cited by 1 publication

References 8 publications

In silico analysis of a heme-thiolate peroxidase gene discovered in an ectomycorrhizal fungus of Carpathian primeval forest: implications for biotechnological applications

In silico analysis of a heme-thiolate peroxidase gene discovered in an ectomycorrhizal fungus of Carpathian primeval forest: implications for biotechnological applications

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