Molecular Dynamics Simulation Reveals the Mechanism of Substrate Recognition by Lignin-Degrading Enzymes.

ABSTRACT: Lignin, the most abundant aromatic biopolymer, represents a key renewable feedstock for sustainable biorefineries, yet its structural complexity poses a formidable challenge for enzymatic degradation. While ligninolytic enzymes such as laccases (LACs), lignin peroxidases (LiPs), and manganese peroxidases (MnPs) exhibit remarkable catalytic versatility, the molecular mechanisms underlying their ability to balance substrate specificity and structural flexibility remain unresolved. Here, we employed all-atom molecular dynamics (MD) simulations and virtual mutagenesis to dissect the dynamic interactions between these enzymes and lignin model compound (β-O-4-linked H-type dimers). Our simulations revealed a dual recognition mechanism in which polar residues (such as Asp, Glu, Arg and His) forme

SUBMITTER: Ma X 

PROVIDER: S-EPMC12525479 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature