Abstract 1175 Steady-state kinetic studies L-DOPA 2,3-Dioxygenase with lignin metabolite 3,4-dihydroxyhydrocinnamic acid and its 6-substituted derivatives

Lignin, a complex polymer in plant cell walls, is an abundant carbon source with an energy-rich structure and promising pharmaceutical applications, including antibiotic synthesis. Central to lignin biodegradation, dioxygenase enzymes catalyze catecholic ring cleavage-a reaction exploited in nature to produce bioactive compounds, such as lincomycin. However, the substrate scope and reactivity of these enzymes remain underexplored. This study evaluates steady-state kinetic parameters (KM, kcat, and ksp) of L-DOPA 2,3-dioxygenase enzymes from S.