Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches
We reconstructed the molecular phylogeny of heme containing peroxygenases that are known as very versatile biocatalysts. These oxidoreductases capable of mainly oxyfunctionalizations constitute the peroxidase–peroxygenase superfamily. Our representative reconstruction revealed a high diversity but a...
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MDPI AG
2022-05-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/11/5/1011 |
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| author | Marcel Zámocký Jana Harichová |
| author_facet | Marcel Zámocký Jana Harichová |
| author_sort | Marcel Zámocký |
| collection | DOAJ |
| description | We reconstructed the molecular phylogeny of heme containing peroxygenases that are known as very versatile biocatalysts. These oxidoreductases capable of mainly oxyfunctionalizations constitute the peroxidase–peroxygenase superfamily. Our representative reconstruction revealed a high diversity but also well conserved sequence motifs within rather short protein molecules. Corresponding genes coding for heme thiolate peroxidases with peroxygenase activity were detected only among various lower eukaryotes. Most of them originate in the kingdom of fungi. However, it seems to be obvious that these <i>htp</i> genes are present not only among fungal Dikarya but they are distributed also in the clades of Mucoromycota and Chytridiomycota with deep ancient evolutionary origins. Moreover, there is also a distinct clade formed mainly by phytopathogenic Stramenopiles where even HTP sequences from Amoebozoa can be found. The phylogenetically older heme peroxygenases are mostly intracellular, but the later evolution gave a preference for secretory proteins mainly among pathogenic fungi. We also analyzed the conservation of typical structural features within various resolved clades of peroxygenases. The presented output of our phylogenetic analysis may be useful in the rational design of specifically modified peroxygenases for various future biotech applications. |
| first_indexed | 2024-03-10T03:25:17Z |
| format | Article |
| id | doaj.art-561011382c1140df900f11ba89ed68cf |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-10T03:25:17Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-561011382c1140df900f11ba89ed68cf2023-11-23T09:53:01ZengMDPI AGAntioxidants2076-39212022-05-01115101110.3390/antiox11051011Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved BranchesMarcel Zámocký0Jana Harichová1Laboratory for Phylogenomic Ecology, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská Cesta 21, SK-84551 Bratislava, SlovakiaLaboratory for Phylogenomic Ecology, Institute of Molecular Biology, Slovak Academy of Sciences, Dúbravská Cesta 21, SK-84551 Bratislava, SlovakiaWe reconstructed the molecular phylogeny of heme containing peroxygenases that are known as very versatile biocatalysts. These oxidoreductases capable of mainly oxyfunctionalizations constitute the peroxidase–peroxygenase superfamily. Our representative reconstruction revealed a high diversity but also well conserved sequence motifs within rather short protein molecules. Corresponding genes coding for heme thiolate peroxidases with peroxygenase activity were detected only among various lower eukaryotes. Most of them originate in the kingdom of fungi. However, it seems to be obvious that these <i>htp</i> genes are present not only among fungal Dikarya but they are distributed also in the clades of Mucoromycota and Chytridiomycota with deep ancient evolutionary origins. Moreover, there is also a distinct clade formed mainly by phytopathogenic Stramenopiles where even HTP sequences from Amoebozoa can be found. The phylogenetically older heme peroxygenases are mostly intracellular, but the later evolution gave a preference for secretory proteins mainly among pathogenic fungi. We also analyzed the conservation of typical structural features within various resolved clades of peroxygenases. The presented output of our phylogenetic analysis may be useful in the rational design of specifically modified peroxygenases for various future biotech applications.https://www.mdpi.com/2076-3921/11/5/1011heme thiolate peroxidaseperoxygenaseperoxidase–peroxygenase superfamilyearly diverging fungiStramenopilesmolecular evolution |
| spellingShingle | Marcel Zámocký Jana Harichová Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches Antioxidants heme thiolate peroxidase peroxygenase peroxidase–peroxygenase superfamily early diverging fungi Stramenopiles molecular evolution |
| title | Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches |
| title_full | Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches |
| title_fullStr | Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches |
| title_full_unstemmed | Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches |
| title_short | Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches |
| title_sort | evolution of heme peroxygenases ancient roots and later evolved branches |
| topic | heme thiolate peroxidase peroxygenase peroxidase–peroxygenase superfamily early diverging fungi Stramenopiles molecular evolution |
| url | https://www.mdpi.com/2076-3921/11/5/1011 |
| work_keys_str_mv | AT marcelzamocky evolutionofhemeperoxygenasesancientrootsandlaterevolvedbranches AT janaharichova evolutionofhemeperoxygenasesancientrootsandlaterevolvedbranches |