Evidence map›Paper›PMID 27088303›Full record

ArticleJournal of the American Chemical Society2016

Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin A.

Swapnil V Ghodge, Kristen A Biernat, Sarah Jane Bassett, Matthew R Redinbo, Albert A Bowers

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 2025
    Review
  3. Review
  4. Indolylamide Macrocyclization by aOrganic letters · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Exploring the Post-translational Enzymology of PaaA by mRNA Display.Journal of the American Chemical Society · 2020
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. 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

5 authors.

Swapnil V GhodgeDivision of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill , Eshelmann School of Pharmacy, Chapel Hill, North Carolina 27599, United States.
Kristen A BiernatDepartment of Chemistry, University of North Carolina at Chapel Hill , Chapel Hill, North Carolina 27599, United States.
Sarah Jane BassettDivision of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill , Eshelmann School of Pharmacy, Chapel Hill, North Carolina 27599, United States.
Matthew R RedinboDepartment of Chemistry, University of North Carolina at Chapel Hill , Chapel Hill, North Carolina 27599, United States.
Albert A BowersDivision of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill , Eshelmann School of Pharmacy, Chapel Hill, North Carolina 27599, United States.

Funding

Improving CPT-11 Efficacy Using Structural BiologyR01CA098468 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI REDINBO, MATTHEW R · 2003 to 2018
$3.9M
NCI NIH HHS R01 CA098468
6 · The paper itself

Abstract

Pantocin A (PA) is a member of the growing family of ribosomally encoded and post-translationally modified peptide natural products (RiPPs). PA is much smaller than most known RiPPs, a tripeptide with a tight bicyclic core that appears to be cleaved from the middle of a larger 30-residue precursor peptide. We show here that the enzyme PaaA catalyzes the double dehydration and decarboxylation of two glutamic acid residues in the 30-residue precursor PaaP. Further truncates of PaaP leader and follower peptide sequences demonstrate the different impacts of these two regions on PaaA-mediated tailoring and delineate an essential role for the follower sequence in the decarboxylation step. The crystal structure of apo PaaA is reported, allowing identification of structural features that set PaaA apart from other homologous enzymes that typically do not catalyze such extended post-translational chemistry. Together, these data reveal how additional chemistry can be extracted from a ubiquitous enzyme family toward ribosomally derived peptide natural product biosynthesis and suggest that more examples of such enzymes likely exist in untapped genomic space.

Indexed as

Protein Processing, Post-TranslationalBridged Bicyclo CompoundsCrystallography, X-RayDecarboxylationGlycopeptidesBridged Bicyclo CompoundsGlycopeptidespantocin A

Identifiers

PMID27088303
PMCPMC4955399

What OpenQuestion holds

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Registered trials

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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.