Evidence map›Paper›PMID 29725007›Full record

ArticleNature communications2018

A distributive peptide cyclase processes multiple microviridin core peptides within a single polypeptide substrate.

Yi Zhang, Kunhua Li, Guang Yang, Joshua L McBride, Steven D Bruner, Yousong Ding

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Article
  2. Secondary metabolism ofApplied and environmental microbiology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. RiPP Enzymes for Biosynthetically Derived Cyclic Peptide Libraries.Methods in molecular biology (Clifton, N.J.) · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. First Report onToxins · 2021
    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.

Yi ZhangDepartment of Medicinal Chemistry, Center for Natural Products, Drug Discovery and Development, College of Pharmacy, University of Florida, Gainesville, Florida, 32610, USA.
Kunhua LiDepartment of Chemistry, University of Florida, Gainesville, Florida, 32611, USA.ORCID http://orcid.org/0000-0002-9139-4257
Guang YangDepartment of Medicinal Chemistry, Center for Natural Products, Drug Discovery and Development, College of Pharmacy, University of Florida, Gainesville, Florida, 32610, USA.
Joshua L McBrideDepartment of Medicinal Chemistry, Center for Natural Products, Drug Discovery and Development, College of Pharmacy, University of Florida, Gainesville, Florida, 32610, USA.
Steven D BrunerDepartment of Chemistry, University of Florida, Gainesville, Florida, 32611, USA.
Yousong DingDepartment of Medicinal Chemistry, Center for Natural Products, Drug Discovery and Development, College of Pharmacy, University of Florida, Gainesville, Florida, 32610, USA. yding@cop.ufl.edu.ORCID http://orcid.org/0000-0001-8610-0659

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are an important family of natural products. Their biosynthesis follows a common scheme in which the leader peptide of a precursor peptide guides the modifications of a single core peptide. Here we describe biochemical studies of the processing of multiple core peptides within a precursor peptide, rare in RiPP biosynthesis. In a cyanobacterial microviridin pathway, an ATP-grasp ligase, AMdnC, installs up to two macrolactones on each of the three core peptides within AMdnA. The enzyme catalysis occurs in a distributive fashion and follows an unstrict N-to-C overall directionality, but a strict order in macrolactonizing each core peptide. Furthermore, AMdnC is catalytically versatile to process unnatural substrates carrying one to four core peptides, and kinetic studies provide insights into its catalytic properties. Collectively, our results reveal a distinct biosynthetic logic of RiPPs, opening up the possibility of modular production via synthetic biology approaches.

Indexed as

Amino Acid SequenceCatalysisCyclizationDepsipeptidesEnzymesKineticsLactonesProtein ConformationProtein Sorting SignalsRibosomesSubstrate SpecificityDepsipeptidesEnzymesLactonesProtein Sorting Signals

Identifiers

PMID29725007
PMCPMC5934393

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.