Matters of class: coming of age of class III and IV lanthipeptides-Reference-Cited by-同舟云学术

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Matters of class: coming of age of class III and IV lanthipeptides

Published:2020 Issue:3 Volume:1 Page:110-127
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Hegemann Julian D.¹²³⁴⁵^ORCID,Süssmuth Roderich D.¹²³⁴⁵^ORCID

Affiliation:

1. Institute of Chemistry

2. Technische Universität Berlin

3. Straße des 17. Juni 124

4. Berlin

5. Germany

Abstract

In this review, we give a concise overview of the known biosynthetic princples of class III and IV lanthipeptide synthtases.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2020/CB/D0CB00073F

Reference75 articles.

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

2. Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes

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

4. Structure and mechanism of lanthipeptide biosynthetic enzymes

5. Structure and Mechanism of the Lantibiotic Cyclase Involved in Nisin Biosynthesis

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2. Heterologous Biosynthesis of New Lanthipeptides Nocardiopeptins with an Unprecedented Bridging Pattern of Lanthionine and Labionin;ACS Chemical Biology;2024-09-09

3. Mechanistic insights into lanthipeptide modification by a distinct subclass of LanKC enzyme that forms dimers;Nature Communications;2024-08-17

4. Heterologous Expression Facilitates the Production and Characterization of a Class III Lanthipeptide with Coupled Labionin Cross-Links in Sponge-Associated Streptomyces rochei MB037;ACS Chemical Biology;2024-08-15

5. Insights into the production and evolution of lantibiotics from a computational analysis of peptides associated with the lanthipeptide cyclase domain;Royal Society Open Science;2024-07

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