How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery-Reference-Cited by-同舟云学术

How a Subfamily of Radical S-Adenosylmethionine Enzymes Became a Mainstay of Ribosomally Synthesized and Post-translationally Modified Peptide Discovery

Published:2021-12-02 Issue: Volume: Page:
ISSN:2694-2437
Container-title:ACS Bio & Med Chem Au
language:en
Short-container-title:ACS Bio Med Chem Au

Author:

Mendauletova Aigera¹,Kostenko Anastasiia¹,Lien Yi¹,Latham John¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, University of Denver, Denver, Colorado 80210, United States

Funder

Division of Chemistry

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acsbiomedchemau.1c00045

Reference68 articles.

1. New developments in RiPP discovery, enzymology and engineering

2. Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature

3. PqqD Is a Novel Peptide Chaperone That Forms a Ternary Complex with the Radical S-Adenosylmethionine Protein PqqE in the Pyrroloquinoline Quinone Biosynthetic Pathway

4. A prevalent peptide-binding domain guides ribosomal natural product biosynthesis

5. Structure and mechanism of the tRNA-dependent lantibiotic dehydratase NisB

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