Evidence map›Paper›PMID 31216342›Full record

ArticlePloS one2019

A new lipoxygenase from the agaric fungus Agrocybe aegerita: Biochemical characterization and kinetic properties.

Dominik Karrer, Martin Rühl

Abstract read
In one paragraph

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
  2. Improved catalytic performance and molecular insight for lipoxygenase fromFrontiers in bioengineering and biotechnology · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. 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

2 authors.

Dominik KarrerInstitute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Giessen, Hesse, Germany.
Martin RühlInstitute of Food Chemistry and Food Biotechnology, Justus Liebig University Giessen, Giessen, Hesse, Germany.ORCID 0000-0001-8274-8175

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxylipins are metabolites with a variety of biological functions. However, the biosynthetic pathway is widely unknown. It is considered that the first step is the oxygenation of polyunsaturated fatty acids like linoleic acid. Therefore, a lipoxygenase (LOX) from the edible basidiomycete Agrocybe aegerita was investigated. The AaeLOX4 was heterologously expressed in E. coli and purified via affinity chromatography and gel filtration. Biochemical properties and kinetic parameters of the purified AaeLOX4 were determined with linoleic acid and linolenic acid as substrates. The obtained Km, vmax and kcat values for linoleic acid were 295.5 μM, 16.5 μM · min-1 · mg-1 and 103.9 s-1, respectively. For linolenic acid Km, vmax and kcat values of 634.2 μM, 19.5 μM · min-1 · mg-1 and 18.3 s-1 were calculated. Maximum activities were observed at pH 7.5 and 25 °C. The main product of linoleic acid conversion was identified with normal-phase HPLC. This analysis revealed an explicit production of 13-hydroperoxy-9,11-octadecadienoic acid (13-HPOD). The experimental regio specificity is underpinned by the amino acid residues W384, F450, R594 and V635 considered relevant for regio specificity in LOX. In conclusion, HPLC-analysis and alignments revealed that AaeLOX4 is a 13-LOX.

Indexed as

AgrocybeAmino Acid MotifsCatalytic DomainFungal ProteinsKineticsLinoleic AcidLipoxygenasesSubstrate SpecificityFungal ProteinsLinoleic AcidLipoxygenases

Identifiers

PMID31216342
PMCPMC6584016

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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.