ArticleScientific reports2017
Fungal Hybrid B heme peroxidases - unique fusions of a heme peroxidase domain with a carbohydrate-binding domain.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Molecular Insights into the Activation of a Fungal Copper Radical Oxidase by Peroxidases.Chem & bio engineering · 2026Article
- Cancer therapy with engineered nanozymes: from molecular design to tumour-responsive catalysis.Nanomedicine (London, England) · 2025Review
- Insights into the fungal secretomes and their roles in the formation and stabilization of the biogenic silver nanoparticles.RSC advances · 2025Article
- Tandem metalloenzymes gate plant cell entry by pathogenic fungi.Science advances · 2022Article
- Article
- Hybrid Heme Peroxidases from Rice Blast FungusAntioxidants (Basel, Switzerland) · 2020Article
- Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Heme peroxidases, essential peroxide converting oxidoreductases are divided into four independently evolved superfamilies. Within the largest one - the peroxidase-catalase superfamily - two hybrid lineages were described recently. Whereas Hybrid A heme peroxidases represent intermediate enzymes between ascorbate peroxidases and cytochrome c peroxidases, Hybrid B heme peroxidases are unique fusion proteins comprised of a conserved N-terminal heme peroxidase domain and a C-terminal domain of various sugar binding motifs. So far these peculiar peroxidases are only found in the kingdom of Fungi. Here we present a phylogenetic reconstruction of the whole superfamily with focus on Hybrid B peroxidases. We analyse the domain assembly and putative structure and function of the newly discovered oligosaccharide binding domains. Two distinct carbohydrate binding modules (CBM21 and CBM34) are shown to occur in phytopathogenic ascomycetous orthologs of Hybrid B heme peroxidases only. Based on multiple sequence alignment and homology modeling the structure-function relationships are discussed with respect to physiological function. A concerted action of peroxide cleavage with specific cell-wall carbohydrate binding can support phytopathogens survival within the plant host.
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Registered trials
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