Catabolism of acetosyringone and co-metabolic transformation of 2,4,6-trichlorophenol by a novel FAD-dependent monooxygenase.
Engl T, Jakubova L, Skrob Z, Campeggi S, Skala R
Summary
6.8/10Scientists discovered a new bacterial enzyme that breaks down acetosyringone, a plant compound found in lignin. This enzyme works through a different mechanism than previously known pathways, which could improve our understanding of how bacteria decompose plant material in soil and potentially enable better composting and biofuel production.
Key Findings
Novel FAD-dependent monooxygenase (AsdA) catalyzes direct aromatic core hydroxylation of acetosyringone
This represents a mechanistically distinct pathway compared to the previously documented side-chain modification route
Enzyme identified through metagenomic analysis of bacterial consortium using acetosyringone as sole carbon source
Original Abstract
Acetosyringone (AS), a prototypical syringyl-type monomer of lignin, functions as a model compound for the study of microbial catabolism of S-lignin-derived aromatics. In this study, we present the discovery of a novel metabolic pathway for AS catabolism, initiated by a previously uncharacterized FAD-dependent oxidoreductase, designated AsdA. In contrast to the sole previously documented AS funneling route, which entails side chain modification and conversion to syringic acid, AsdA catalyzes direct hydroxylation of the aromatic core. This represents a mechanistically distinct entry into central metabolism. The identification of this enzyme was achieved through metagenomic and functional analyses of a bacterial consortium enriched on AS as the sole carbon source. The consortium, predominantly comprising