Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Poljovka, Andrej, Musil, Miloš, Bednář, David, Chovanová, Katarína, Bauerová-Hlinková, Vladena, Bellová, Jana, Kohútová, Lenka, Baráth, Peter, Zámocký, Marcel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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
_version_ 1785079206107938816
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
work_keys_str_mv AT poljovkaandrej comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT musilmilos comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT bednardavid comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT chovanovakatarina comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT bauerovahlinkovavladena comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT bellovajana comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT kohutovalenka comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT barathpeter comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties
AT zamockymarcel comparisonoffungalthermophilicandmesophiliccatalaseperoxidasesfortheirantioxidativeproperties