Stuffed Methyltransferase Catalyzes the Penultimate Step of Pyochelin Biosynthesis.

ABSTRACT: Nonribosomal peptide synthetases use tailoring domains to incorporate chemical diversity into the final natural product. A structurally unique set of tailoring domains are found to be stuffed within adenylation domains and have only recently begun to be characterized. PchF is the NRPS termination module in pyochelin biosynthesis and includes a stuffed methyltransferase domain responsible for S-adenosylmethionine (AdoMet)-dependent N-methylation. Recent studies of stuffed methyltransferase domains propose a model in which methylation occurs on amino acids after adenylation and thiolation rather than after condensation to the nascent peptide chain. Herein, we characterize the adenylation and stuffed methyltransferase didomain of PchF through the synthesis and use of substrate analogues, stea

SUBMITTER: Ronnebaum TA 

PROVIDER: S-EPMC6372355 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature