Evidence map›Paper›PMID 26534965›Full record

ArticleThe Journal of biological chemistry2015

Elucidating the Specificity Determinants of the AtxE2 Lasso Peptide Isopeptidase.

Mikhail O Maksimov, Joseph D Koos, Chuhan Zong, Bozhena Lisko, A James Link

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. 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
2.0field-weighted citation impact, top 11% 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, 30 citations in OpenAlex.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020
    Review
  8. Article
  9. Lasso Peptides: Heterologous Production and Potential Medical Application.Frontiers in bioengineering and biotechnology · 2020
    Review
  10. Article
  11. Genome mining for lasso peptides: past, present, and future.Journal of industrial microbiology & biotechnology · 2019
    Review
  12. Article
  13. Article
  14. Lasso Peptide Benenodin-1 Is a Thermally Actuated [1]Rotaxane Switch.Journal of the American Chemical Society · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  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 at 1 institution in 2 countries.

Mikhail O MaksimovFrom the Departments of Chemical and Biological Engineering.
Joseph D KoosMolecular Biology, and.
Chuhan ZongChemistry, Princeton University, Princeton, New Jersey 08544.
Bozhena LiskoFrom the Departments of Chemical and Biological Engineering.
A James LinkFrom the Departments of Chemical and Biological Engineering, Molecular Biology, and ajlink@princeton.edu.ORCID http://orcid.org/0000-0001-5066-9691
Princeton University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Lasso Peptide DiscoveryR01GM107036 · NIGMS · PRINCETON UNIVERSITY · PI LINK, AARON JAMES · 2014 to 2022
$2.9M
NIGMS NIH HHS R01 GM107036NIGMS NIH HHS T32 GM007388NIGMS NIH HHS T32 GM7388
6 · The paper itself

Abstract

Lasso peptide isopeptidase is an enzyme that specifically hydrolyzes the isopeptide bond of lasso peptides, rendering these peptides linear. To carry out a detailed structure-activity analysis of the lasso peptide isopeptidase AtxE2 from Asticcacaulis excentricus, we solved NMR structures of its substrates astexin-2 and astexin-3. Using in vitro enzyme assays, we show that the C-terminal tail portion of these peptides is dispensable with regards to isopeptidase activity. A collection of astexin-2 and astexin-3 variants with alanine substitutions at each position within the ring and the loop was constructed, and we showed that all of these peptides except for one were cleaved by the isopeptidase. Thus, much like the lasso peptide biosynthetic enzymes, lasso peptide isopeptidase has broad substrate specificity. Quantitative analysis of the cleavage reactions indicated that alanine substitutions in loop positions of these peptides led to reduced cleavage, suggesting that the loop is serving as a recognition element for the isopeptidase.

Indexed as

AlphaproteobacteriaAmino Acid SequenceBacterial ProteinsBiocatalysisCarbon-Nitrogen LyasesCrystallography, X-RayModels, MolecularPeptidesSubstrate SpecificityBacterial ProteinsCarbon-Nitrogen LyasesisopeptidasePeptidesenzyme processingnatural product biosynthesisnuclear magnetic resonance (NMR)peptidaseserine proteasestructure-function

Identifiers

PMID26534965
PMCPMC4692210
OpenAlexW2299810412

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.