8C9V

O-methyltransferase from Desulfuromonas acetoxidans

8C9V の概要

• エントリーDOI: 10.2210/pdb8c9v/pdb
• 分子名称: O-methyltransferase, family 3, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Desulfuromonas acetoxidans DSM 684
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22665.76

構造登録者

Zhang, L.,Groves, M.R. (登録日: 2023-01-23, 公開日: 2023-04-05, 最終更新日: 2023-09-20)

主引用文献

Sokolova, N.,Zhang, L.,Deravi, S.,Oerlemans, R.,Groves, M.R.,Haslinger, K.
Structural Characterization and Extended Substrate Scope Analysis of Two Mg 2+ -Dependent O-Methyltransferases from Bacteria.
Chembiochem, 24:e202300076-e202300076, 2023

PubMed Abstract: Oxygen-directed methylation is a ubiquitous tailoring reaction in natural product pathways catalysed by O-methyltransferases (OMTs). Promiscuous OMT biocatalysts are thus a valuable asset in the toolkit for sustainable synthesis and optimization of known bioactive scaffolds for drug development. Here, we characterized the enzymatic properties and substrate scope of two bacterial OMTs from Desulforomonas acetoxidans and Streptomyces avermitilis and determined their crystal structures. Both OMTs methylated a wide range of catechol-like substrates, including flavonoids, coumarins, hydroxybenzoic acids, and their respective aldehydes, an anthraquinone and an indole. One enzyme also accepted a steroid. The product range included pharmaceutically relevant compounds such as (iso)fraxidin, iso(scopoletin), chrysoeriol, alizarin 1-methyl ether, and 2-methoxyestradiol. Interestingly, certain non-catechol flavonoids and hydroxybenzoic acids were also methylated. This study expands the knowledge on substrate preference and structural diversity of bacterial catechol OMTs and paves the way for their use in (combinatorial) pathway engineering.

PubMed: 36942619
DOI: 10.1002/cbic.202300076

実験手法

X-RAY DIFFRACTION (1.5 Å)