8c9s | pdb_00008c9s

Catechol O-methyltransferase from Streptomyces avermitilis in complex with SAH

spinqualitylabelsall models 8c9s, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8c9s is a 2 chain structure with sequence from Streptomyces avermitilis MA-4680 = NBRC 14893. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BAQ, MG, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q82B68_STRAW Publication Abstract from PubMed 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. Structural Characterization and Extended Substrate Scope Analysis of Two Mg(2+) -Dependent O-Methyltransferases from Bacteria.,Sokolova N, Zhang L, Deravi S, Oerlemans R, Groves MR, Haslinger K Chembiochem. 2023 Mar 21:e202300076. doi: 10.1002/cbic.202300076. PMID:36942619 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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