Structural highlights
Publication Abstract from PubMedWhite-rot fungi (WRF) are the most efficient lignin-degrading organisms in nature. However, their capacity to use lignin-related aromatic compounds, such as 4-hydroxybenzoate, as carbon sources has only been described recently. Previously, the hydroxyquinol pathway was proposed for the bioconversion of these compounds in fungi, but gene- and structure-function relationships of the full enzymatic pathway remain uncharacterized in any single fungal species. Here, we characterize seven enzymes from two WRF, Trametes versicolor and Gelatoporia subvermispora, which constitute a four-enzyme cascade from 4-hydroxybenzoate to beta-ketoadipate via the hydroxyquinol pathway. Furthermore, we solve the crystal structure of four of these enzymes and identify mechanistic differences with the closest bacterial and fungal structural homologs. Overall, this research expands our understanding of aromatic catabolism by WRF and establishes an alternative strategy for the conversion of lignin-related compounds to the valuable molecule beta-ketoadipate, contributing to the development of biological processes for lignin valorization. Biochemical and structural characterization of enzymes in the 4-hydroxybenzoate catabolic pathway of lignin-degrading white-rot fungi.,Kuatsjah E, Schwartz A, Zahn M, Tornesakis K, Kellermyer ZA, Ingraham MA, Woodworth SP, Ramirez KJ, Cox PA, Pickford AR, Salvachua D Cell Rep. 2024 Nov 25;43(12):115002. doi: 10.1016/j.celrep.2024.115002. PMID:39589922[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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