Comparison of Fungal Thermophilic and Mesophilic
Catalase-Peroxidases for Their Antioxidative Properties

J 2023

Comparison of Fungal Thermophilic and Mesophilic Catalase-Peroxidases for Their Antioxidative Properties

POLJOVKA, Andrej, Miloš MUSIL, David BEDNÁŘ, Katarina CHOVANOVA, Vladena BAUEROVA-HLINKOVA et. al.

Basic information

Original name

Comparison of Fungal Thermophilic and Mesophilic Catalase-Peroxidases for Their Antioxidative Properties

Authors

POLJOVKA, Andrej, Miloš MUSIL (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, guarantor, belonging to the institution), Katarina CHOVANOVA, Vladena BAUEROVA-HLINKOVA, Jana BELLOVA, Lenka KOHUTOVA, Peter BARATH and Marcel ZAMOCKY

Edition

Antioxidants, Basel, MDPI, 2023, 2076-3921

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Switzerland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 7.000 in 2022

RIV identification code

RIV/00216224:14310/23:00131488

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.3390/antiox12071382

UT WoS

001034982300001

Keywords in English

peroxidase-catalase superfamily; heme catalase; bifunctional enzyme; reactive oxygen species; oxidative stress

Abstract

V originále

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.

Links

EF17_043/0009632, research and development project

Name: CETOCOEN Excellence

LM2023055, research and development project

Name: Česká národní infrastruktura pro biologická data

Investor: Ministry of Education, Youth and Sports of the CR, ELIXIR-CZ: Czech National Infrastructure for Biological Data

LM2023069, research and development project

Name: Výzkumná infrastruktura RECETOX

Investor: Ministry of Education, Youth and Sports of the CR, RECETOX research infrastructure

Citovat

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.

@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.

Detailed Information on Publication Record