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These enzymes exhibit a marked preference for decolorizing recalcitrant anthraquinone dyes, setting them apart from other peroxidases; however, the molecular mechanism underlying this preference remains to be elucidated. This study explores the catalytic profile of recombinant\n                      <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                      -DyP4, a dye-decolorizing peroxidase from\n                      <jats:italic toggle=\"yes\">Irpex lacteus<\/jats:italic>\n                      F17, to clarify the molecular basis of its substrate preference. We found that\n                      <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                      -DyP4 exhibits remarkable H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      tolerance in the oxidation of anthraquinone dyes, maintaining approximately 50% activity even at H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      concentrations above 20 mM, while its activity toward phenolic substrates decreases by 50% at only 0.6 mM H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      concentration. These results demonstrate the distinct capability of\n                      <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                      -DyP4 to catalyze anthraquinone dyes at high H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      . Analysis of the intermediates of Reactive Blue 19 transformation showed that this catalytic ability is linked to the bifunctional activity of\n                      <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                      -DyP4: the enzyme couples peroxidative oxidation with hydrolytic cleavage to rapidly scavenge H\n                      <jats:sub>2<\/jats:sub>\n                      O\n                      <jats:sub>2<\/jats:sub>\n                      , thereby averting self-inactivation of the enzyme. In contrast, guaiacol oxidation by\n                      <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                      -DyP4 followed the canonical peroxidase route, proceeding exclusively via C\u2013C radical coupling to yield oligomeric products. These findings provide a mechanistic rationale for the intrinsic preference of DyPs for anthraquinone-based dyes and highlight\n                      <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                      -DyP4 as a resilient, high-performance biocatalyst for remediating dye-contaminated wastewater.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        Here, we reveal that the long-sought specificity of dye-decolorizing peroxidase (DyP) for anthraquinone dyes arises from a bifunctional mechanism orchestrated by\n                        <jats:italic toggle=\"yes\">Il<\/jats:italic>\n                        -DyP4, encompassing both peroxidase-mediated oxidation and hydrolytic cleavage. Elucidating this dual chemistry not only redefines the catalytic behavior of the DyP family but also provides a mechanistic cornerstone for engineering robust biocatalysts to eliminate recalcitrant dye pollutants in industrial wastewater.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/aem.00282-26","type":"journal-article","created":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T13:00:37Z","timestamp":1776862837000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":1,"title":["Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase"],"prefix":"10.1128","volume":"92","author":[{"given":"Peilin","family":"Lin","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05th6yx34","id-type":"ROR","asserted-by":"publisher"}],"name":"School of Life Sciences and 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