ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
Structure-Guided Engineering of a Promiscuous O-Methyltransferase for a SAM Regeneration Biocatalysis Platform of Methylated Pharmaceuticals.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Structural insights into a dual-substrate O-methyltransferase reveal the enzymatic mechanism of parallel paeonol biosynthesis.Nature communications · 2026Article
- Structural Elucidation and Engineering of the (S)-scoulerine 2-O-Methyltransferase Enabling Regioselective Epiberberine Biosynthesis in Coptis chinensis.Plant biotechnology journal · 2026Article
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Authors and funding
12 authors.
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Abstract
O-Methylation catalyzed by plant O-methyltransferase plays a crucial role in both drug design and biosynthesis of natural products. However, their practical applications are often restricted by strict substrate specificity and a strong dependence on the expensive methyl donor S-adenosyl-L-methionine (SAM). Herein, an O-methyltransferase, SmOMT, is identified from the medicinal plant Selaginella moellendorffii, exhibiting substrate promiscuity and regioselectivity. SmOMT catalyzed the methylation of 25 structurally diverse substrates and demonstrated detectable N-methylation activity. Combined ternary complex structure and molecular dynamics studies of SmOMT elucidate its catalytic and regioselectivity mechanisms. A double mutant, SmOMT
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