Unveiling the molecular basis of selective fluorination of SAM-dependent fluorinases.

ABSTRACT: S-Adenosylmethionine (SAM)-dependent fluorinases have emerged as environmentally friendly enzymatic alternatives for organofluorine chemical synthesis. However, their use remains limited by their rarity; only 16 fluorinases have been found in nature so far. Here we report two new fluorinases, FLA^Sbac from Streptosporangiales bacterium and a modified FLA^Adig_Nter from Actinoplanes digitatis. Through molecular dynamics (MD) simulations, we have identified the crucial roles of the SAM-binding site and an ion-egress site (IES) for fluorination reaction, particularly regarding its preference for fluoride ions. We have validated these findings by testing mutants of the two new fluorinases and the known fluorinase from Streptomyces sp. MA37 (FLA

SUBMITTER: Verma RK 

PROVIDER: S-EPMC12080486 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature