絞り込み

16638

広告

Distinct autocatalytic α- N-methylating precursors expand the borosin RiPP family of peptide natural products.

著者 Quijano MR , Zach C , Miller FS , Lee AR , Imani AS , Künzler M , Freeman MF
J Am Chem Soc.2019 May 22 ; ():.
この記事をPubMed上で見るPubMedで表示
この記事をGoogle翻訳上で見る Google翻訳で開く

スターを付ける スターを付ける     (9view , 0users)

Full Text Sources

Backbone N-methylations impart several favorable characteristics to peptides including increased proteolytic stability and membrane permeability. Nonetheless, amide bond N-methylations incorporated as post-translational modifications are scarce in nature, and were first demonstrated in 2017 for a single set of fungal metabolites. Here we expand on our previous discovery of iterative, autocatalytic α- N-methylating precursor proteins in the borosin family of ribosomally encoded peptide natural products. We identify over fifty putative pathways in a variety of ascomycete and basidiomycete fungi, and functionally validate nearly a dozen new self-α- N-methylating catalysts. Significant differences in precursor size, architecture, and core peptide properties subdivide this new peptide family into three discrete structural types. Lastly, using targeted genomics, we link the biosynthetic origins of the potent antineoplastic gymnopeptides to the borosin natural product family. This work highlights the metabolic potential of fungi for ribosomally synthesized peptide natural products.
PMID: 31117659 [PubMed - as supplied by publisher]
印刷用ページを開く Endnote用テキストダウンロード