Hybrid Heme Peroxidases from Rice Blast Fungus Magnaporthe oryzae Involved in Defence against Oxidative Stress

Zámocký, Marcel; Kamlárová, Anna; Maresch, Daniel; Chovanová, Katarína; Harichová, Jana; Furtmüller, Paul G.

doi:10.3390/antiox9080655

Cited by 10 publications

(6 citation statements)

References 41 publications

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“…Related heme peroxidases from the same protein superfamily that do not possess this PTM are not able to dismutate hydrogen peroxide efficiently although they possess a very similar architecture of the active center. They can only react in the peroxidase pathway by oxidizing various substrates with concomitant reduction of hydrogen peroxide to water as was shown for their various purified representatives, e.g., [31,35,36]. Moreover, the results recorded from monitored protein thermal unfolding demonstrate that after introduction of these single point mutations in (originally) thermostable KatG, the overall stability of both produced mutants was negatively influenced in comparison to the rather high folding stability of the wild type enzyme.…”

Section: Discussionmentioning

confidence: 86%

“…Second, a specifically developed method allows the removal of colored stamps from various types of papers [34] with the usage of CthedisKatG. Recently, we presented typical features of fungal hybrid B heme peroxidases [35,36] and also of fungal heme peroxygenases [37] that reveal a slightly different reaction mechanism to classical peroxidases. In contrast to all the above mentioned peroxidase families, bifunctional catalase-peroxidases possess, in addition to a highly variable peroxidase activity (comprising many different natural and synthetic substrates), a significant catalase activity.…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2023

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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.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

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

et al. 2023

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“…It shall be noted that this reaction scheme is typical for all kinds of peroxidases and “A” in this equation can be numerous 1- or 2-electron donors of various types e.g., methanol, ethanol, formic acid, or phenols and their substituted derivatives as well as aromatic amines [ 37 ]. Bifunctional enzymes named catalase-peroxidases (abbreviated as KatGs) also exist (E.C.…”

Section: Resultsmentioning

confidence: 99%

Parallel Molecular Evolution of Catalases and Superoxide Dismutases—Focus on Thermophilic Fungal Genomes

et al. 2020

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Catalases (CAT) and superoxide dismutases (SOD) represent two main groups of enzymatic antioxidants that are present in almost all aerobic organisms and even in certain anaerobes. They are closely interconnected in the catabolism of reactive oxygen species because one product of SOD reaction (hydrogen peroxide) is the main substrate of CAT reaction finally leading to harmless products (i.e., molecular oxygen and water). It is therefore interesting to compare the molecular evolution of corresponding gene families. We have used a phylogenomic approach to elucidate the evolutionary relationships among these two main enzymatic antioxidants with a focus on the genomes of thermophilic fungi. Distinct gene families coding for CuZnSODs, FeMnSODs, and heme catalases are very abundant in thermophilic Ascomycota. Here, the presented results demonstrate that whereas superoxide dismutase genes remained rather constant during long-term evolution, the total count of heme catalase genes was reduced in thermophilic fungi in comparison with their mesophilic counterparts. We demonstrate here, for the newly discovered ascomycetous genes coding for thermophilic superoxide dismutases and catalases (originating from our sequencing project), the expression patterns of corresponding mRNA transcripts and further analyze translated protein sequences. Our results provide important implications for the physiology of reactive oxygen species metabolism in eukaryotic cells at elevated temperatures.

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“…It is also likely that the accumulation of spontaneous natural mutations eventually culminated in the establishment of the families that we encounter nowadays. Additionally, the occurrence of APX-CCP proteins in some species and the functional diversity observed in such proteins provide strong support for this model [ 52 , 53 ]. In this scenario, the identification of hybrid proteins is another outstanding piece of evidence of this evolutionary process.…”

Section: Discussionmentioning

confidence: 99%

Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida

et al. 2021

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Ascorbate peroxidases (APX) are class I members of the Peroxidase-Catalase superfamily, a large group of evolutionarily related but rather divergent enzymes. Through mining in public databases, unusual subsets of APX homologs were identified, disclosing the existence of two yet uncharacterized families of peroxidases named ascorbate peroxidase-related (APX-R) and ascorbate peroxidase-like (APX-L). As APX, APX-R harbor all catalytic residues required for peroxidatic activity. Nevertheless, proteins of this family do not contain residues known to be critical for ascorbate binding and therefore cannot use it as an electron donor. On the other hand, APX-L proteins not only lack ascorbate-binding residues, but also every other residue known to be essential for peroxidase activity. Through a molecular phylogenetic analysis performed with sequences derived from basal Archaeplastida, the present study discloses the existence of hybrid proteins, which combine features of these three families. The results here presented show that the prevalence of hybrid proteins varies among distinct groups of organisms, accounting for up to 33% of total APX homologs in species of green algae. The analysis of this heterogeneous group of proteins sheds light on the origin of APX-R and APX-L and suggests the occurrence of a process characterized by the progressive deterioration of ascorbate-binding and catalytic sites towards neofunctionalization.

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Hybrid Heme Peroxidases from Rice Blast Fungus Magnaporthe oryzae Involved in Defence against Oxidative Stress

Cited by 10 publications

References 41 publications

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

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

Parallel Molecular Evolution of Catalases and Superoxide Dismutases—Focus on Thermophilic Fungal Genomes

Ascorbate Peroxidase Neofunctionalization at the Origin of APX-R and APX-L: Evidence from Basal Archaeplastida

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