Evidence map›Paper›PMID 16517758›Full record

ArticleThe Plant cell2006

FaQR, required for the biosynthesis of the strawberry flavor compound 4-hydroxy-2,5-dimethyl-3(2H)-furanone, encodes an enone oxidoreductase.

Thomas Raab, Juan Antonio López-Ráez, Dorothée Klein, Jose Luis Caballero, Enriqueta Moyano, Wilfried Schwab, Juan Muñoz-Blanco

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

55 citing papers in PubMed, 178 citations in OpenAlex.

  1. Article
  2. Article
  3. Promiscuous Transferases Malonylate Furaneol Glucoside inJournal of agricultural and food chemistry · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Construction of aFood science & nutrition · 2024
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Importance of FaWRKY71 in Strawberry (International journal of molecular sciences · 2022
    Article
  16. Article
  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

7 authors at 2 institutions in 2 countries.

Thomas RaabInstitute of Pharmacy and Food Chemistry, University of Würzburg, 97074 Würzburg, Germany.
Juan Antonio López-Ráez
Dorothée Klein
Jose Luis Caballero
Enriqueta Moyano
Wilfried Schwab
Juan Muñoz-Blanco
University of Córdoba · ESUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The flavor of strawberry (Fragaria x ananassa) fruit is dominated by an uncommon group of aroma compounds with a 2,5-dimethyl-3(H)-furanone structure. We report the characterization of an enzyme involved in the biosynthesis of 4-hydroxy-2,5-dimethyl-3(2H)-furanone (HDMF; Furaneol), the key flavor compound in strawberries. Protein extracts were partially purified, and the observed distribution of enzymatic activity correlated with the presence of a single polypeptide of approximately 37 kD. Sequence analysis of two peptide fragments showed total identity with the protein sequence of a strongly ripening-induced, auxin-dependent putative quinone oxidoreductase, Fragaria x ananassa quinone oxidoreductase (FaQR). The open reading frame of the FaQR cDNA consists of 969 bp encoding a 322-amino acid protein with a calculated molecular mass of 34.3 kD. Laser capture microdissection followed by RNA extraction and amplification demonstrated the presence of FaQR mRNA in parenchyma tissue of the strawberry fruit. The FaQR protein was functionally expressed in Escherichia coli, and the monomer catalyzed the formation of HDMF. After chemical synthesis and liquid chromatography-tandem mass spectrometry analysis, 4-hydroxy-5-methyl-2-methylene-3(2H)-furanone was confirmed as a substrate of FaQR and the natural precursor of HDMF. This study demonstrates the function of the FaQR enzyme in the biosynthesis of HDMF as enone oxidoreductase and provides a foundation for the improvement of strawberry flavor and the biotechnological production of HDMF.

Indexed as

TasteAmino Acid SequenceComputational BiologyConserved SequenceFragariaFruitFuransIndoleacetic AcidsKineticsMolecular Sequence DataOxidoreductases Acting on CH-CH Group DonorsPeptide FragmentsPlant ProteinsReverse Transcriptase Polymerase Chain ReactionRNA, PlantSequence AlignmentfuraneolFuransIndoleacetic AcidsOxidoreductases Acting on CH-CH Group DonorsPeptide FragmentsPlant ProteinsRNA, Plant

Identifiers

PMID16517758
PMCPMC1425863
OpenAlexW2159979717

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.