ArticleJournal of the American Chemical Society2012
An engineered lantibiotic synthetase that does not require a leader peptide on its substrate.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 97 citations in OpenAlex.
- Advancements in the Application of Ribosomally Synthesized and Post-Translationally Modified Peptides (RiPPs).Biomolecules · 2024Pooled it
- Repositioning the Leader Peptide in Graspetide Biosynthesis.Journal of the American Chemical Society · 2026Article
- A Versatile Enzymatic Pathway for Modification of Peptide C‑Termini.ACS central science · 2025Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- RiPP Enzymes for Biosynthetically Derived Cyclic Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Genome Mining for New Enzyme Chemistry.ACS catalysis · 2024Review
- An Autocatalytic Peptide Cyclase Improves Fidelity and Yield of Circular Peptides In Vivo and In Vitro.ACS synthetic biology · 2024Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- Engineering lanthipeptides by introducing a large variety of RiPP modifications to obtain new-to-nature bioactive peptides.FEMS microbiology reviews · 2023Review
- Peptidase Activation by a Leader Peptide-Bound RiPP Recognition Element.Biochemistry · 2023Article
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Biosynthesis and characterization of fuscimiditide, an aspartimidylated graspetide.Nature chemistry · 2022Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Accessing Diverse Pyridine-Based Macrocyclic Peptides by a Two-Site Recognition Pathway.Journal of the American Chemical Society · 2022Article
- Redirecting RiPP Biosynthetic Enzymes to Proteins and Backbone-Modified Substrates.ACS central science · 2022Article
- Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.Nature chemical biology · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Substrate Recognition by the Class II Lanthipeptide Synthetase HalM2.ACS chemical biology · 2020Article
- A Structural View on the Maturation of Lanthipeptides.Frontiers in microbiology · 2020Review
- Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Ribosomally synthesized and post-translationally modified peptides are a rapidly expanding class of natural products. They are typically biosynthesized by modification of a C-terminal segment of the precursor peptide (the core peptide). The precursor peptide also contains an N-terminal leader peptide that is required to guide the biosynthetic enzymes. For bioengineering purposes, the leader peptide is beneficial because it allows promiscuous activity of the biosynthetic enzymes with respect to modification of the core peptide sequence. However, the leader peptide also presents drawbacks as it needs to be present on the core peptide and then removed in a later step. We show that fusing the leader peptide for the lantibiotic lacticin 481 to its biosynthetic enzyme LctM allows the protein to act on core peptides without a leader peptide. We illustrate the use of this methodology for preparation of improved lacticin 481 analogues containing non-proteinogenic amino acids.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.