Functional characterization of a novel <i>p</i>-coumarate 3-hydroxylase from <i>Trametes versicolor</i>.

ABSTRACT: Lignin degradation by white-rot fungi proceeds through oxidative depolymerization of lignin polymers, followed by metabolism of the resulting low-molecular-weight aromatic fragments. Among these, the catabolism of the hydroxyphenyl (H) unit of p-coumaric acid (p-CA) remains poorly understood in fungi. Here, we investigated the metabolism of p-CA by Trametes versicolor. Two group A flavoprotein monooxygenases (FPMOs), TvMNX3 and TvMNX4, catalyzed the hydroxylation of p-CA to caffeic acid. Recombinant expression and biochemical analyses revealed that TvMNX4 exhibited the highest catalytic efficiency toward both p-CA and 4-hydroxybenzoic acid, suggesting that it plays a major role in these hydroxylation reactions. Both enzymes als

SUBMITTER: Hamajima L 

PROVIDER: S-EPMC12915361 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature