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The article discusses a novel mechanism for enhancing P450 demethylase activity through engineered key gating residues. The research focuses on the cytochrome CYP199A4 monooxygenase from Rhodopseudomonas palustris strain HaA2, which catalyzes the demethylation of lignin monomer derivatives. The study highlights the importance of exploring new O-demethylases through gene mining and improving existing enzymes through protein engineering to overcome limitations in substrate specificity, reaction mechanisms, and reliance on cofactors.
Researchers reveal novel mechanism of enhanced P450 demethylase activity through engineered key gating residues
June 14, 2024
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A crucial step in the degradation and utilization of lignin is the process of O-demethylation of lignin monomers, facilitated by O-demethylases. Current O-demethylases face challenges such as limited substrate specificity, unclear reaction mechanisms, and a lack of reductase chaperones. Therefore, the exploration of new O-demethylases through gene mining and the improvement of existing O-demethylases through protein engineering are of great importance.
The cytochrome CYP199A4 monooxygenase from Rhodopseudomonas palustris strain HaA2 is one of the few cytochrome P450 enzymes known to catalyze the demethylation of lignin monomer derivatives. However, its demethylation activity depends on the presence of the nicotinamide cofactor NADH and a reducing chaperone protein.
A team