Evidence map›Paper›PMID 19389704›Full record

ArticleThe Journal of biological chemistry2009

Processing of the phalloidin proprotein by prolyl oligopeptidase from the mushroom Conocybe albipes.

Hong Luo, Heather E Hallen-Adams, Jonathan D Walton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. 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
1.6field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Myxarylin: TotalJournal of the American Chemical Society · 2026
    Article
  2. Molecular Phylogeny and Morphology Reveal Four New Species ofJournal of fungi (Basel, Switzerland) · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Mechanisms of cyanobactin biosynthesis.Current opinion in chemical biology · 2016
    Review
  11. Production of (15)N-labeled α-amanitin in Galerina marginata.Toxicon : official journal of the International Society on Toxinology · 2015
    Article
  12. Article
  13. The chemistry and biology of theta defensins.Angewandte Chemie (International ed. in English) · 2014
    Review
  14. Prospecting genomes for lasso peptides.Journal of industrial microbiology & biotechnology · 2014
    Review
  15. Review
  16. Ribosomal biosynthesis of α-amanitin in Galerina marginata.Fungal genetics and biology : FG & B · 2012
    Article
  17. Article
  18. Review
  19. Review
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 at 1 institution in 1 country.

Hong LuoDepartment of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824, USA.
Heather E Hallen-Adams
Jonathan D Walton
Michigan State University · US

Funding

BIOSYNTHESIS OF THE CYCLIC PEPTIDE TOXINS OF AMANITA MUSHROOMSR01GM088274 · NIGMS · MICHIGAN STATE UNIVERSITY · PI WALTON, JONATHAN · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM088274
6 · The paper itself

Abstract

The peptide toxins of poisonous Amanita mushrooms are bicyclic octapeptides (amatoxins) or heptapeptides (phallotoxins). In Amanita bisporigera, alpha-amanitin and phallacidin are synthesized as 35- and 34-amino acid proproteins, respectively, in which the amino acid sequences found in the mature toxins are flanked by conserved amino acid sequences. The presence of invariant Pro residues immediately upstream of the toxin regions and as the last predicted amino acid in the toxin regions themselves suggests that a Pro-specific peptidase is responsible for the initial post-translational processing of the Amanita toxin proproteins. We purified an enzyme from the phalloidin-producing mushroom Conocybe albipes that cleaves a synthetic 22-mer phalloidin peptide to release the mature toxin peptide (AWLATCP). Mass spectrometric analysis of the purified protein combined with isolation and sequencing of the encoding gene indicates that the responsible processing enzyme is a member of the prolyl oligopeptidase (POP) subfamily of proteases (EC 3.4.21.26). The processing enzyme was able to use the chromogenic POP substrate benzyloxycarbonyl-Gly-Pro-p-nitroanilide and was inhibited by the specific POP inhibitor benzyloxycarbonyl-Pro-prolinal. Both Pro bonds in the proprotein are cleaved by the same enzyme, with the C-terminal Pro bond cleaved first or much faster than the N-terminal Pro bond. Transient accumulation of the N-terminal intermediate indicates that cleavage is not strongly processive. A synthetic peptide representing the phallacidin proprotein was also cleaved by the POP of C. albipes, but a precursor of amanitin (which is not made by C. albipes) was cleaved inefficiently.

Indexed as

Amino Acid SequenceBasidiomycotaFruiting Bodies, FungalFungal ProteinsKineticsMolecular Sequence DataPhalloidineProlyl OligopeptidasesProtein PrecursorsProteomicsSerine EndopeptidasesFungal ProteinsPhalloidineProlyl OligopeptidasesProtein PrecursorsSerine Endopeptidases

Identifiers

PMID19389704
PMCPMC2709354
OpenAlexW2130302956

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.