O-Methyltransferase-Mediated Incorporation of a β-Amino Acid in Lanthipeptides.

ABSTRACT: Lanthipeptides represent a large class of cyclic natural products defined by the presence of lanthionine (Lan) and methyllanthionine (MeLan) cross-links. With the advances in DNA sequencing technologies and genome mining tools, new biosynthetic enzymes capable of installing unusual structural features are continuously being discovered. In this study, we investigated an O-methyltransferase that is a member of the most prominent auxiliary enzyme family associated with class I lanthipeptide biosynthetic gene clusters. Despite the prevalence of these enzymes, their function has not been established. Herein, we demonstrate that the O-methyltransferase OlvS_A encoded in the olv gene cluster from Streptomyces olivaceus NRRL B-3009 catalyzes the rearrangement

SUBMITTER: Acedo JZ 

PROVIDER: S-EPMC6812601 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature