Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.

ABSTRACT: DyP-type peroxidases (DyPs) are microbial enzymes that catalyze the oxidation of a wide range of substrates, including synthetic dyes, lignin-derived compounds, and metals, such as Mn²⁺ and Fe²⁺, and have enormous biotechnological potential in biorefineries. However, many questions on the molecular basis of enzyme function and stability remain unanswered. In this work, high-resolution structures of PpDyP wild-type and two engineered variants (6E10 and 29E4) generated by directed evolution were obtained. The X-ray crystal structures revealed the typical ferredoxin-like folds, with three heme access pathways, two tunnels, and one cavity, limited by three long loops including catalytic residues. Variant 6E10 displays significantly increased loops' flexibility that

SUBMITTER: Borges PT 

PROVIDER: S-EPMC9334217 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature