Evidence map›Paper›PMID 33586286›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Genome-Mining-Based Discovery of the Cyclic Peptide Tolypamide and TolF, a Ser/Thr Forward O-Prenyltransferase.

Mugilarasi Purushothaman, Snigdha Sarkar, Maho Morita, Muriel Gugger, Eric W Schmidt, Brandon I Morinaka

Open access · bronzeAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
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

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Biosynthesis of guanidine-containing natural products in cyanobacteria.Journal of industrial microbiology & biotechnology · 2024
    Review
  6. Article
  7. Article
  8. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Biochemical characterization of a cyanobactin arginine-Chemical communications (Cambridge, England) · 2022
    Article
  14. Article
  15. Review
  16. Catalysts for the Enzymatic Lipidation of Peptides.Accounts of chemical research · 2022
    Review
  17. Article
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

6 authors at 4 institutions in 4 countries.

Mugilarasi PurushothamanDepartment of Pharmacy, National University of Singapore, 18 Science Dr 4, Singapore, 117543, Singapore.
Snigdha SarkarDepartment of Medicinal Chemistry, University of Utah, Salt Lake City, UT, 84112, USA.ORCID 0000-0003-4551-0314
Maho MoritaLaboratory of Chemical Biology of Natural Products, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa, Nagoya, 464-8601, Japan.
Muriel GuggerInstitut Pasteur, Collection des Cyanobactéries, Département de Microbiologie, 75015, Paris, France.ORCID 0000-0001-6728-1976
Eric W SchmidtDepartment of Medicinal Chemistry, University of Utah, Salt Lake City, UT, 84112, USA.ORCID 0000-0001-5839-694X
Brandon I MorinakaDepartment of Pharmacy, National University of Singapore, 18 Science Dr 4, Singapore, 117543, Singapore.ORCID 0000-0001-8239-619X
National University of Singapore · SGUniversity of Utah · USInstitut Pasteur · FRNagoya University · JP

Funding

Symbiosis and Chemical Diversity GenerationR35GM122521 · NIGMS · UNIVERSITY OF UTAH · PI SCHMIDT, ERIC W · 2017 to 2021
$2.9M
NIGMS NIH HHS R35 GM122521
6 · The paper itself

Abstract

Cyanobactins comprise a widespread group of peptide metabolites produced by cyanobacteria that are often diversified by post-translational prenylation. Several enzymes have been identified in cyanobactin biosynthetic pathways that carry out chemically diverse prenylation reactions, representing a resource for the discovery of post-translational alkylating agents. Here, genome mining was used to identify orphan cyanobactin prenyltransferases, leading to the isolation of tolypamide from the freshwater cyanobacterium Tolypothrix sp. The structure of tolypamide was confirmed by spectroscopic methods, degradation, and enzymatic total synthesis. Tolypamide is forward-prenylated on a threonine residue, representing an unprecedented post-translational modification. Biochemical characterization of the cognate enzyme TolF revealed a prenyltransferase with strict selectivity for forward O-prenylation of serine or threonine but with relaxed substrate selectivity for flanking peptide sequences. Since cyanobactin pathways often exhibit exceptionally broad substrate tolerance, these enzymes represent robust tools for synthetic biology.

Indexed as

Bacterial ProteinsCyanobacteriaDimethylallyltranstransferaseMolecular StructurePeptides, CyclicThreonineBacterial ProteinsDimethylallyltranstransferasePeptides, CyclicThreoninebiosynthesisgenome miningnatural productspeptidesprenylationRiPPs

Identifiers

PMID33586286
PMCPMC8011950
OpenAlexW3132597650

What OpenQuestion holds

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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.