ArticleProceedings of the National Academy of Sciences of the United States of America2023
The mechanism of thia-Michael addition catalyzed by LanC enzymes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Loss of LanC-like proteins delays post-injury regeneration of aging skeletal muscles.bioRxiv : the preprint server for biology · 2026Article
- Embleporicin: A Novel Class I Lanthipeptide from the ActinobacteriaAntibiotics (Basel, Switzerland) · 2024Article
- Substrate Specificity of a Methyltransferase Involved in the Biosynthesis of the Lantibiotic Cacaoidin.Biochemistry · 2024Article
- Characterization of a LanC-free pathway for the formation of an ll-MeLan residue and anChemical science · 2024Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- Clickable Glutathione-Based Identification of Cysteine Glutathionylation.Current protocols · 2023Article
- Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
In both eukarya and bacteria, the addition of Cys to dehydroalanine (Dha) and dehydrobutyrine (Dhb) occurs in various biological processes. In bacteria, intramolecular thia-Michael addition catalyzed by lanthipeptide cyclases (LanC) proteins or protein domains gives rise to a class of natural products called lanthipeptides. In eukarya, dehydroamino acids in signaling proteins are introduced by effector proteins produced by pathogens like
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