Structural Characterization and Extended Substrate Scope Analysis of Two Mg²⁺‐Dependent O‐Methyltransferases from Bacteria**

Abstract

Table of contentsTwo promiscuous O-methyltransferases from bacteria were found to methylate a panel of catechol substrates towards high-value medicinal compounds. Surprisingly, the non-catechol substrates 5hydroxyflavonoids and o-hydroxybenzoic acids/aldehydes were also methylated at low conversion rates. The crystal structures reveal potential target sites for enzyme engineering for biocatalytic applications.

Recent developments in the enzymatic modifications of steroid scaffolds

“…18B). 147 Welander and coworkers reported sterol C-24 methyltransferases (SMTs) from both sponges and yetuncultured bacteria that catalyzed the methylation of desmosterol (108) to generate C-24 methyl sterols, including 24-methyl-enecholesterol and (epi)codisterol (109 to 111) (Fig. 18C).…”

Enzymatic Oxy‐ and Amino‐Functionalization in Biocatalytic Cascade Synthesis: Recent Advances and Future Perspectives

“…For instance, Sokolova et al. recently characterized two catechol O ‐methyltransferases (COMTs) from two bacterial species, Desulforomonas acetoxidans (DesAOMT) and Streptomyces avermitilis (StrAOMT) [75] . Both enzymes were biochemically characterized and their activity was investigated with a range of potential substrates, revealing that both COMTs accept catechol‐like and non‐catechol‐like molecules.…”

“…[73,74] For instance, Sokolova et al recently characterized two catechol O-methyltransferases (COMTs) from two bacterial species, Desulforomonas acetoxidans (DesAOMT) and Streptomyces avermitilis (StrAOMT). [75] Both enzymes were biochemically characterized and their activity was investigated with a range of potential substrates, revealing that both COMTs accept catechol-like and noncatechol-like molecules. Structural analysis revealed a Mg 2 + binding site, as well as structure similarities with other OMTs, like the characteristic SAM-binding pocket of StrAOMT, but also significant differences like the missing N-terminal helix in DesAOMT.…”