Evidence map›Paper›PMID 26783260›Full record

ArticleThe Journal of biological chemistry2016

Crystal Structure of Manganese Lipoxygenase of the Rice Blast Fungus Magnaporthe oryzae.

Anneli Wennman, Ernst H Oliw, Saeid Karkehabadi, Yang Chen

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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.6field-weighted citation impact, top 3% 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

28 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  3. Allosteric properties of mammalian ALOX15 orthologs.The Journal of biological chemistry · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Impact ofBiochemistry · 2024
    Article
  8. Article
  9. Biochemistry · 2023
    Article
  10. Genome-wide identification and analysis ofFrontiers in genetics · 2022
    Article
  11. Article
  12. Biochemical Characterization of 13-Lipoxygenases ofInternational journal of molecular sciences · 2021
    Article
  13. Genomic Analyses ofJournal of fungi (Basel, Switzerland) · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Anneli WennmanFrom the Department of Pharmaceutical Biosciences, Uppsala University Biomedical Center, SE-751 24 Uppsala, Sweden.
Ernst H OliwFrom the Department of Pharmaceutical Biosciences, Uppsala University Biomedical Center, SE-751 24 Uppsala, Sweden Ernst.oliw@farmbio.uu.se.
Saeid KarkehabadiFrom the Department of Pharmaceutical Biosciences, Uppsala University Biomedical Center, SE-751 24 Uppsala, Sweden.
Yang ChenFrom the Department of Pharmaceutical Biosciences, Uppsala University Biomedical Center, SE-751 24 Uppsala, Sweden.
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipoxygenases (LOX) are non-heme metal enzymes, which oxidize polyunsaturated fatty acids to hydroperoxides. All LOX belong to the same gene family, and they are widely distributed. LOX of animals, plants, and prokaryotes contain iron as the catalytic metal, whereas fungi express LOX with iron or with manganese. Little is known about metal selection by LOX and the adjustment of the redox potentials of their protein-bound catalytic metals. Thirteen three-dimensional structures of animal, plant, and prokaryotic FeLOX are available, but none of MnLOX. The MnLOX of the most important plant pathogen, the rice blast fungusMagnaporthe oryzae(Mo), was expressed inPichia pastoris.Mo-MnLOX was deglycosylated, purified to homogeneity, and subjected to crystal screening and x-ray diffraction. The structure was solved by sulfur and manganese single wavelength anomalous dispersion to a resolution of 2.0 Å. The manganese coordinating sphere is similar to iron ligands of coral 8R-LOX and soybean LOX-1 but is not overlapping. The Asn-473 is positioned on a short loop (Asn-Gln-Gly-Glu-Pro) instead of an α-helix and forms hydrogen bonds with Gln-281. Comparison with FeLOX suggests that Phe-332 and Phe-525 might contribute to the unique suprafacial hydrogen abstraction and oxygenation mechanism of Mo-MnLOX by controlling oxygen access to the pentadiene radical. Modeling suggests that Arg-525 is positioned close to Arg-182 of 8R-LOX, and both residues likely tether the carboxylate group of the substrate. An oxygen channel could not be identified. We conclude that Mo-MnLOX illustrates a partly unique variation of the structural theme of FeLOX.

Indexed as

Crystallography, X-RayFatty AcidsLipoxygenaseMagnaportheModels, MolecularOryzaOxidation-ReductionProtein ConformationFatty AcidsLipoxygenasemanganese lipoxygenasecrystal structureenzyme mechanismfatty acid oxidationlipoxygenase pathwaymetalloenzyme

Identifiers

PMID26783260
PMCPMC4825015
OpenAlexW1780928835

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.