| POLJOVKA, Andrej, Miloš MUSIL, David BEDNÁŘ, Katarina CHOVANOVA, Vladena BAUEROVA-HLINKOVA, Jana BELLOVA, Lenka KOHUTOVA, Peter BARATH and Marcel ZAMOCKY. Comparison of Fungal Thermophilic and Mesophilic Catalase-Peroxidases for Their Antioxidative Properties. Antioxidants. Basel: MDPI, 2023, vol. 12, No 7, p. 1-19. ISSN 2076-3921. Available from: https://dx.doi.org/10.3390/antiox12071382. |
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@article{2303823,
author = {Poljovka, Andrej and Musil, Miloš and Bednář, David and Chovanova, Katarina and BauerovaandHlinkova, Vladena and Bellova, Jana and Kohutova, Lenka and Barath, Peter and Zamocky, Marcel},
article_location = {Basel},
article_number = {7},
doi = {http://dx.doi.org/10.3390/antiox12071382},
keywords = {peroxidase-catalase superfamily; heme catalase; bifunctional enzyme; reactive oxygen species; oxidative stress},
language = {eng},
issn = {2076-3921},
journal = {Antioxidants},
title = {Comparison of Fungal Thermophilic and Mesophilic Catalase-Peroxidases for Their Antioxidative Properties},
url = {https://www.mdpi.com/2076-3921/12/7/1382},
volume = {12},
year = {2023}
}
TY - JOUR
ID - 2303823
AU - Poljovka, Andrej - Musil, Miloš - Bednář, David - Chovanova, Katarina - Bauerova-Hlinkova, Vladena - Bellova, Jana - Kohutova, Lenka - Barath, Peter - Zamocky, Marcel
PY - 2023
TI - Comparison of Fungal Thermophilic and Mesophilic Catalase-Peroxidases for Their Antioxidative Properties
JF - Antioxidants
VL - 12
IS - 7
SP - 1-19
EP - 1-19
PB - MDPI
SN - 20763921
KW - peroxidase-catalase superfamily
KW - heme catalase
KW - bifunctional enzyme
KW - reactive oxygen species
KW - oxidative stress
UR - https://www.mdpi.com/2076-3921/12/7/1382
N2 - 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.
ER -
POLJOVKA, Andrej, Miloš MUSIL, David BEDNÁŘ, Katarina CHOVANOVA, Vladena BAUEROVA-HLINKOVA, Jana BELLOVA, Lenka KOHUTOVA, Peter BARATH and Marcel ZAMOCKY. Comparison of Fungal Thermophilic and Mesophilic Catalase-Peroxidases for Their Antioxidative Properties. \textit{Antioxidants}. Basel: MDPI, 2023, vol.~12, No~7, p.~1-19. ISSN~2076-3921. Available from: https://dx.doi.org/10.3390/antiox12071382.
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