Structure of methyltransferase RedM that forms the dimethylpyrrolinium of the bisindole reductasporine.

ABSTRACT: Bisindoles are biologically active natural products that arise from the oxidative dimerization of two molecules of l-tryptophan. In bacterial bisindole pathways, a core set of transformations is followed by the action of diverse tailoring enzymes that catalyze reactions that lead to diverse bisindole products. Among bisindoles, reductasporine is distinct due to its dimethylpyrrolinium structure. Its previously reported biosynthetic gene cluster encodes two unique tailoring enzymes, the imine reductase RedE and the dimethyltransferase RedM, which were shown to produce reductasporine from a common bisindole intermediate in recombinant E. coli. To gain more insight into the unique tailoring enzymes in reductasporine assembly, we reconstituted the biosynthetic pathway to reductasporine in vitr

SUBMITTER: Daniel-Ivad P 

PROVIDER: S-EPMC10784701 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature