Evidence map›Paper›PMID 27703013›Full record

ArticleThe Journal of biological chemistry2016

PvdN Enzyme Catalyzes a Periplasmic Pyoverdine Modification.

Michael T Ringel, Gerald Dräger, Thomas Brüser

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Pyoverdine-Mediated Killing ofInternational journal of molecular sciences · 2020
    Article
  13. Review
  14. The Journal of biological chemistry · 2018
    Article
  15. The biosynthesis of pyoverdines.Microbial cell (Graz, Austria) · 2018
    Review
  16. Article
  17. Article
  18. Pyridoxal-5'-phosphate as an oxygenase cofactor: Discovery of a carboxamide-forming, α-amino acid monooxygenase-decarboxylase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. The periplasmic transaminase PtaA ofThe Journal of biological chemistry · 2017
    Article
  20. 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.

Michael T RingelFrom the Institute of Microbiology, Leibniz Universität Hannover, Herrenhäuser Straße 2, 30419 Hannover and.
Gerald Drägerthe Institute of Organic Chemistry, Leibniz Universität Hannover, Schneiderberg 1 B, 30167 Hannover, Germany.
Thomas BrüserFrom the Institute of Microbiology, Leibniz Universität Hannover, Herrenhäuser Straße 2, 30419 Hannover and brueser@ifmb.uni-hannover.de.
Leibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyoverdines are high affinity siderophores produced by a broad range of pseudomonads to enhance growth under iron deficiency. They are especially relevant for pathogenic and mutualistic strains that inhabit iron-limited environments. Pyoverdines are generated from non-ribosomally synthesized highly modified peptides. They all contain an aromatic chromophore that is formed in the periplasm by intramolecular cyclization steps. Although the cytoplasmic peptide synthesis and side-chain modifications are well characterized, the periplasmic maturation steps are far from understood. Out of five periplasmic enzymes, PvdM, PvdN, PvdO, PvdP, and PvdQ, functions have been attributed only to PvdP and PvdQ. The other three enzymes are also regarded as essential for siderophore biosynthesis. The structure of PvdN has been solved recently, but no function could be assigned. Here we present the first in-frame deletion of the PvdN-encoding gene. Unexpectedly, PvdN turned out to be required for a specific modification of pyoverdine, whereas the overall amount of fluorescent pyoverdines was not altered by the mutation. The mutant strain grew normally under iron-limiting conditions. Mass spectrometry identified the PvdN-dependent modification as a transformation of the N-terminal glutamic acid to a succinamide. We postulate a pathway for this transformation catalyzed by the enzyme PvdN, which is most likely functional in the case of all pyoverdines.

Indexed as

AmidesGene DeletionGlutamic AcidOligopeptidesPeriplasmPeriplasmic ProteinsPseudomonas fluorescensSuccinatesAmidesGlutamic AcidOligopeptidesPeriplasmic ProteinspyoverdinsuccinamideSuccinatesdecarboxylaseenzymeironperiplasmic tailoringPseudomonas fluorescenspyoverdinespyridoxal phosphatesiderophoresiderophore maturation

Identifiers

PMID27703013
PMCPMC5104919
OpenAlexW2528072464

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.