Evidence map›Paper›PMID 19786119›Full record

ArticleBiochimica et biophysica acta2010

Omega-3 fatty acids are oxygenated at the n-7 carbon by the lipoxygenase domain of a fusion protein in the cyanobacterium Acaryochloris marina.

Benlian Gao, William E Boeglin, Alan R Brash

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.5field-weighted citation impact, top 33% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Intricate Evolution of Multifunctional Lipoxygenase in Red Algae.International journal of molecular sciences · 2024
    Article
  5. Discovery of α-Linolenic Acid 16(International journal of molecular sciences · 2023
    Article
  6. Article
  7. Applications of Microbial Enzymes in Food Industry.Food technology and biotechnology · 2018
    Review
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
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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.

Benlian GaoDepartment of Pharmacology, and the Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, TN 37232, USA.
William E Boeglin
Alan R Brash
Vanderbilt University · US

Funding

Novel Catalases and their ProductsR01GM074888 · NIGMS · VANDERBILT UNIVERSITY · PI BRASH, ALAN R. · 2006 to 2013
$2.4M
NIGMS NIH HHS GM 074888NIGMS NIH HHS R01 GM074888
6 · The paper itself

Abstract

Lipoxygenases (LOX) are found in most organisms that contain polyunsaturated fatty acids, usually existing as individual genes although occasionally encoded as a fusion protein with a catalase-related hemoprotein. Such a fusion protein occurs in the cyanobacterium Acaryochloris marina and herein we report the novel catalytic activity of its LOX domain. The full-length protein and the C-terminal LOX domain were expressed in Escherichia coli, and the catalytic activities characterized by UV, HPLC, GC-MS, and CD. All omega-3 polyunsaturates were oxygenated by the LOX domain at the n-7 position and with R stereospecificity: alpha-linolenic and the most abundant fatty acid in A. marina, stearidonic acid (C18.4omega3), are converted to the corresponding 12R-hydroperoxides, eicosapentaenoic acid to its 14R-hydroperoxide, and docosahexaenoic acid to its 16R-hydroperoxide. Omega-6 polyunsaturates were oxygenated at the n-10 position, forming 9R-hydroperoxy-octadecadienoic acid from linoleic acid and 11R-hydroperoxy-eicosatetraenoic acid from arachidonic acid. The metabolic transformation of stearidonic acid by the full-length fusion protein entails its 12R oxygenation with subsequent conversion by the catalase-related domain to a novel allene epoxide, a likely precursor of cyclopentenone fatty acids or other signaling molecules (Gao et al, J. Biol. Chem. 284:22087-98, 2009). Although omega-3 fatty acids and lipoxygenases are of widespread occurrence, this appears to be the first description of a LOX-catalyzed oxygenation that specifically utilizes the terminal pentadiene of omega-3 fatty acids.

Indexed as

Bacterial ProteinsCyanobacteriaFatty Acids, Omega-3KineticsLipoxygenaseProtein Structure, TertiaryRecombinant Fusion ProteinsSubstrate SpecificityBacterial ProteinsFatty Acids, Omega-3LipoxygenaseRecombinant Fusion Proteins

Identifiers

PMID19786119
PMCPMC2787963
OpenAlexW2087833884

What OpenQuestion holds

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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.