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TitleMolecular and Structural Characterization of a Chalcone di--Methyltransferase RdCMT from and Its Application in De Novo Biosynthesis of Farrerol in .
Journal, issue, pagesJ Am Chem Soc, Vol. 147, Issue 20, Page 17132-17143, Year 2025
Publish dateMay 21, 2025
AuthorsMeng Zhang / Yang-Oujie Bao / Zonglin Dai / Zhilan Qian / Haishuang Yu / Jia-Jing Zhou / Yi Chen / Zilong Wang / Kaituo Wang / Menghao Cai / Min Ye /
PubMed AbstractMethylation plays a crucial role in drug design and optimization. While numerous methyltransferases have been characterized from plants, -methyltransferases, particularly those targeting phenolic ...Methylation plays a crucial role in drug design and optimization. While numerous methyltransferases have been characterized from plants, -methyltransferases, particularly those targeting phenolic skeletons, are rare. In this study, we identified a novel di--methyltransferase RdCMT from the medicinal plant . RdCMT catalyzes a sequential two-step 3'-/5'--methylation of naringenin chalcone, leading to the biosynthesis of farrerol. RdCMT exhibited a strict substrate specificity for chalcones. Through combinatorial catalysis, a series of -methylated flavonoids were synthesized. Moreover, farrerol was synthesized de novo in and with yields of 0.4 mg/g (dry weight) and 149.0 mg/L, respectively. The structure of RdCMT was determined using cryo-electron microscopy (cryo-EM), revealing that residues R328 and G296 significantly influence the substrate specificity of RdCMT. This work not only introduces a potent biocatalyst for the preparation of -methylated flavonoids but also offers insights into the catalytic mechanisms of -methyltransferases.
External linksJ Am Chem Soc / PubMed:40331654
MethodsEM (single particle)
Resolution3.42 Å
Structure data

62579

9kus

EMDB-62579, PDB-9kus:
Cryo-EM structure of C-Methyltransferase from Rhododendron dauricum
Method: EM (single particle) / Resolution: 3.42 Å

Source
  • rhododendron dauricum (plant)
KeywordsTRANSFERASE / Methyltransferase / Dimer

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