Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17

Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17

Background: Dye-decolorizing peroxidases (DyPs) represent a novel family of heme peroxidases that use H2O2 as the final electron acceptor to catalyze the oxidation of various organic compounds. A DyP from Irpex lacteus F17 (Il-DyP4, corresponding to GenBank MG209114), obtained by heterologous expres...

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Bibliographic Details
Main Authors: Chen, T. (Author), He, C. (Author), Huang, W. (Author), Jia, R. (Author), Li, L. (Author), Wang, T. (Author), Zhang, Y. (Author)
Format: Article
Language:English
Published: BioMed Central Ltd 2021
Subjects:
amino acid
Amino acids
Biological water treatment
catalysis
Catalytic efficiencies
Catalytic oxidation
Catalytic properties
crystal structure
Crystal structure
Discoloration
dye
Dye-decolorizing peroxidase
Dyes
Dysprosium compounds
Electron paramagnetic resonances (EPR)
Electron spin resonance spectroscopy
enzyme
Enzymes
Fluorine compounds
Function relationships
fungus
Heterologous expression
High-resolution structures
Hydrogen peroxide
Irpex lacteus
Irpex lacteus F17
Molecules
oxidation
Oxidation
Paramagnetic resonance
Phenols
Porphyrins
Site directed mutagenesis
Spatial conformation
Substrates
Substrates’ oxidation
Tryptophan residues
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