ArticleACS chemical biology2019
Mechanistic Studies of the Kinase Domains of Class IV Lanthipeptide Synthetases.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Core-dependent post-translational modifications guide the biosynthesis of a new class of hypermodified peptides.Nature communications · 2023Article
- Identification of peptides from honeybee gut symbionts as potential antimicrobial agents against Melissococcus plutonius.Nature communications · 2023Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.Angewandte Chemie (International ed. in English) · 2022Article
- Mechanistic Studies on Dehydration in Class V Lanthipeptides.ACS chemical biology · 2022Article
- Unexpected Methyllanthionine Stereochemistry in the Morphogenetic Lanthipeptide SapT.Journal of the American Chemical Society · 2022Article
- Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL.Chembiochem : a European journal of chemical biology · 2021Article
- Identification and characterization of andalusicin: N-terminally dimethylated class III lantibiotic fromiScience · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Matters of class: coming of age of class III and IV lanthipeptides.RSC chemical biology · 2020Review
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Lanthipeptides, which belong to the superfamily of ribosomally synthesized and posttranslationally modified peptides (RiPPs), are associated with various interesting biological activities. Lanthipeptides can be subdivided into four classes that are defined by the characteristics of the corresponding posttranslational modification enzymes. Class IV lanthipeptide synthetases consist of an N-terminal lyase, a central kinase, and a C-terminal cyclase domain. Here, we present the first in-depth characterization of such a kinase domain from the globisporin maturation enzyme SgbL that originates from
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