ArticleBiotechnology for biofuels2021
Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17.
Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase.Applied and environmental microbiology · 2026Article
- Degradation and detoxification of aflatoxin B1 by two peroxidase enzymes from Irpex lacteus F17.Bioprocess and biosystems engineering · 2025Article
- Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the ExtremophileMolecules (Basel, Switzerland) · 2024Article
- Exploring the Extreme Acid Tolerance of a Dynamic Protein Nanocage.Biomacromolecules · 2023Article
- Wood-feeding termite gut symbionts as an obscure yet promising source of novel manganese peroxidase-producing oleaginous yeasts intended for azo dye decolorization and biodiesel production.Biotechnology for biofuels · 2021Article
- Direct Electrochemical Generation of Catalytically Competent Oxyferryl Species of Classes I and P Dye Decolorizing Peroxidases.International journal of molecular sciences · 2021Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
backgroundDye-decolorizing peroxidases (DyPs) represent a novel family of heme peroxidases that use H
resultsHere, we obtained a high-resolution structure (2.0 Å, PDB: 7D8M) of Il‑DyP4 with α-helices, anti-parallel β-sheets and one ferric heme cofactor sandwiched between two domains. The crystal structure of Il‑DyP4 revealed two heme access channels leading from the enzyme molecular surface to its heme region, and also showed four conserved amino acid residues forming the pocket for the conversion of hydrogen peroxide into the water molecule. In addition, we found that Trp264 and Trp380, were two important residues with different roles in Il‑DyP4, by using site-directed mutagenesis and an electron paramagnetic resonance (EPR) study. Trp264 is a noncatalytic residue that mainly is used for maintaining the normal spatial conformation of the heme region and the high-spin state of heme Fe
conclusionsThis study is important for better understanding the catalytic properties of fungal DyPs and their structure-function relationships.
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