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Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties
Catalase–peroxidases (KatGs) are unique bifunctional oxidoreductases that contain heme in their active centers allowing both the peroxidatic and catalatic reaction modes. These originally bacterial enzymes are broadly distributed among various fungi allowing them to cope with reactive oxygen species...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10376177/ https://www.ncbi.nlm.nih.gov/pubmed/37507921 http://dx.doi.org/10.3390/antiox12071382 |
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author | Poljovka, Andrej Musil, Miloš Bednář, David Chovanová, Katarína Bauerová-Hlinková, Vladena Bellová, Jana Kohútová, Lenka Baráth, Peter Zámocký, Marcel |
author_facet | Poljovka, Andrej Musil, Miloš Bednář, David Chovanová, Katarína Bauerová-Hlinková, Vladena Bellová, Jana Kohútová, Lenka Baráth, Peter Zámocký, Marcel |
author_sort | Poljovka, Andrej |
collection | PubMed |
description | Catalase–peroxidases (KatGs) are unique bifunctional oxidoreductases that contain heme in their active centers allowing both the peroxidatic and catalatic reaction modes. These originally bacterial enzymes are broadly distributed among various fungi allowing them to cope with reactive oxygen species present in the environment or inside the cells. We used various biophysical, biochemical, and bioinformatics methods to investigate differences between catalase–peroxidases originating in thermophilic and mesophilic fungi from different habitats. Our results indicate that the architecture of the active center with a specific post-translational modification is highly similar in mesophilic and thermophilic KatG and also the peroxidatic acitivity with ABTS, guaiacol, and L-DOPA. However, only the thermophilic variant CthedisKatG reveals increased manganese peroxidase activity at elevated temperatures. The catalatic activity releasing molecular oxygen is comparable between CthedisKatG and mesophilic MagKatG1 over a broad temperature range. Two constructed point mutations in the active center were performed selectively blocking the formation of described post-translational modification in the active center. They exhibited a total loss of catalatic activity and changes in the peroxidatic activity. Our results indicate the capacity of bifunctional heme enzymes in the variable reactivity for potential biotech applications. |
format | Online Article Text |
id | pubmed-10376177 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-103761772023-07-29 Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties Poljovka, Andrej Musil, Miloš Bednář, David Chovanová, Katarína Bauerová-Hlinková, Vladena Bellová, Jana Kohútová, Lenka Baráth, Peter Zámocký, Marcel Antioxidants (Basel) Article Catalase–peroxidases (KatGs) are unique bifunctional oxidoreductases that contain heme in their active centers allowing both the peroxidatic and catalatic reaction modes. These originally bacterial enzymes are broadly distributed among various fungi allowing them to cope with reactive oxygen species present in the environment or inside the cells. We used various biophysical, biochemical, and bioinformatics methods to investigate differences between catalase–peroxidases originating in thermophilic and mesophilic fungi from different habitats. Our results indicate that the architecture of the active center with a specific post-translational modification is highly similar in mesophilic and thermophilic KatG and also the peroxidatic acitivity with ABTS, guaiacol, and L-DOPA. However, only the thermophilic variant CthedisKatG reveals increased manganese peroxidase activity at elevated temperatures. The catalatic activity releasing molecular oxygen is comparable between CthedisKatG and mesophilic MagKatG1 over a broad temperature range. Two constructed point mutations in the active center were performed selectively blocking the formation of described post-translational modification in the active center. They exhibited a total loss of catalatic activity and changes in the peroxidatic activity. Our results indicate the capacity of bifunctional heme enzymes in the variable reactivity for potential biotech applications. MDPI 2023-07-04 /pmc/articles/PMC10376177/ /pubmed/37507921 http://dx.doi.org/10.3390/antiox12071382 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Poljovka, Andrej Musil, Miloš Bednář, David Chovanová, Katarína Bauerová-Hlinková, Vladena Bellová, Jana Kohútová, Lenka Baráth, Peter Zámocký, Marcel Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties |
title | Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties |
title_full | Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties |
title_fullStr | Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties |
title_full_unstemmed | Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties |
title_short | Comparison of Fungal Thermophilic and Mesophilic Catalase–Peroxidases for Their Antioxidative Properties |
title_sort | comparison of fungal thermophilic and mesophilic catalase–peroxidases for their antioxidative properties |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10376177/ https://www.ncbi.nlm.nih.gov/pubmed/37507921 http://dx.doi.org/10.3390/antiox12071382 |
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