4.7 Article

Computational Study of the C5-Hydroxylation Mechanism Catalyzed by the Diiron Monooxygenase PtmU3 as Part of the Platensimycin Biosynthesis

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PtmC Catalyzes the Final Step of Thioplatensimycin, Thioplatencin, and Thioplatensilin Biosynthesis and Expands the Scope of Arylamine N-Acetyltransferases

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Summary: This study presents a detailed investigation of PtmC, an unusual NAT homologue involved in the biosynthesis of thioplatensimycin and related compounds, highlighting its unique role and evolution from canonical NAT scaffold. The findings expand our understanding of enzyme evolution for substrate diversity and provide insights into the activities of NATs in natural product biosynthesis and xenobiotic detoxification.

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