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Title (Primary) First dye-decolorizing peroxidase from an ascomycetous fungus secreted by Xylaria grammica
Author Kimani, V.; Ullrich, R.; Büttner, E.; Herzog, R.; Kellner, H.; Jehmlich, N.; Hofrichter, M.; Liers, C.
Journal Biomolecules
Year 2021
Department MOLSYB
Volume 11
Issue 9
Page From art. 1391
Language englisch
Topic T9 Healthy Planet
Keywords dye-decolorizing peroxidase; Xylaria grammica; ascomycete; Mn2+ oxidation; Mn2+ binding site
Abstract Background: Fungal DyP-type peroxidases have so far been described exclusively for basidiomycetes. Moreover, peroxidases from ascomycetes that oxidize Mn2+ ions are yet not known. Methods: We describe here the physicochemical, biocatalytic, and molecular characterization of a DyP-type peroxidase (DyP, EC from an ascomycetous fungus. Results: The enzyme oxidizes classic peroxidase substrates such as 2,6-DMP but also veratryl alcohol and notably Mn2+ to Mn3+ ions, suggesting a physiological function of this DyP in lignin modification. The KM value (49 µM) indicates that Mn2+ ions bind with high affinity to the XgrDyP protein but their subsequent oxidation into reactive Mn3+ proceeds with moderate efficiency compared to MnPs and VPs. Mn2+ oxidation was most effective at an acidic pH (between 4.0 and 5.0) and a hypothetical surface exposed an Mn2+ binding site comprising three acidic amino acids (two aspartates and one glutamate) could be localized within the hypothetical XgrDyP structure. The oxidation of Mn2+ ions is seemingly supported by four aromatic amino acids that mediate an electron transfer from the surface to the heme center. Conclusions: Our findings shed new light on the possible involvement of DyP-type peroxidases in lignocellulose degradation, especially by fungi that lack prototypical ligninolytic class II peroxidases
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Kimani, V., Ullrich, R., Büttner, E., Herzog, R., Kellner, H., Jehmlich, N., Hofrichter, M., Liers, C. (2021):
First dye-decolorizing peroxidase from an ascomycetous fungus secreted by Xylaria grammica
Biomolecules 11 (9), art. 1391