Evidence map›Paper›PMID 26165156›Full record

ArticleChemistry & biology2015

Modularity of RiPP Enzymes Enables Designed Synthesis of Decorated Peptides.

Debosmita Sardar, Zhenjian Lin, Eric W Schmidt

Abstract readComparative Study
In one paragraph

Article in Chemistry & biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

63 citing papers in PubMed.

  1. Article
  2. De Novo Discovery of Prenylated Macrocyclic Peptide Ligands.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. RiPP Enzymes for Biosynthetically Derived Cyclic Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  7. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  8. Cell-free Biosynthesis of Peptidomimetics.Biotechnology and bioprocess engineering : BBE · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Catalysts for the Enzymatic Lipidation of Peptides.Accounts of chemical research · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Debosmita SardarDepartment of Medicinal Chemistry, University of Utah, 30 South 2000 East, Salt Lake City, UT 84112, USA.
Zhenjian LinDepartment of Medicinal Chemistry, University of Utah, 30 South 2000 East, Salt Lake City, UT 84112, USA.
Eric W SchmidtDepartment of Medicinal Chemistry, University of Utah, 30 South 2000 East, Salt Lake City, UT 84112, USA. Electronic address: ews1@utah.edu.

Funding

Directed posttranslational modifications for drug design and discoveryR01GM102602 · NIGMS · UNIVERSITY OF UTAH · PI SCHMIDT, ERIC W · 2013 to 2016
$1.4M
NIGMS NIH HHS NIH GM102602NIGMS NIH HHS R01 GM102602
6 · The paper itself

Abstract

Macrocyclases and other posttranslational enzymes afford derived peptides with improved properties for pharmaceutical and biotechnological applications. Here, we asked whether multiple posttranslational modifications could be simultaneously controlled and matched to rationally generate new peptide derivatives. We reconstituted the cyanobactin peptide natural products in vitro with up to five different posttranslational enzymes in a single tube. By manipulating the order of addition and identity of enzymes and exploiting their broad-substrate tolerance, we engineered the production of highly unnatural derivatives, including an N-C peptide macrocycle of 22 amino acids in length. In addition to engineering, this work better defines the macrocyclization mechanism, provides the first biochemical demonstration of Ser/Thr posttranslational prenylation, and is the first example of reconstitution of a native, multistep RiPP pathway with multiple enzymes in one pot. Overall, this work demonstrates how the modularity of posttranslational modification enzymes can be used to design and synthesize desirable peptide motifs.

Indexed as

Amino Acid SequenceBacterial ProteinsCyanobacteriaMolecular Sequence DataPeptide HydrolasesPeptides, CyclicProtein Processing, Post-TranslationalProtein Structure, TertiaryBacterial ProteinsPeptide HydrolasesPeptides, Cyclic

Identifiers

PMID26165156
PMCPMC4522240

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Registered trials

None linked

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.