Evidence map›Paper›PMID 16247561›Full record

ArticlePlant molecular biology2005

Functional characterization of a melon alcohol acyl-transferase gene family involved in the biosynthesis of ester volatiles. Identification of the crucial role of a threonine residue for enzyme activity*.

Islam El-Sharkawy, Daniel Manríquez, Francisco B Flores, Farid Regad, Mondher Bouzayen, Alain Latché, Jean-Claude Pech

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
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  17. Alcohol acyltransferases for the biosynthesis of esters.Biotechnology for biofuels and bioproducts · 2023
    Review
  18. Article
  19. Thorough Characterization ofFoods (Basel, Switzerland) · 2023
    Article
  20. Genome-Wide Identification ofLife (Basel, Switzerland) · 2022
    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 1 country.

Islam El-SharkawyUMR 990 INRA/INPT-ENSAT Génomique et Biotechnologie des Fruits, Av. de l'Agrobiopole, BP 32607, F-31326, Castanet-Tolosan Cedex.
Daniel Manríquez
Francisco B Flores
Farid Regad
Mondher Bouzayen
Alain Latché
Jean-Claude Pech
Institut National Polytechnique de Toulouse · FRGenomics and Biotechnology of the Fruits Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Volatile esters, a major class of compounds contributing to the aroma of many fruit, are synthesized by alcohol acyl-transferases (AAT). We demonstrate here that, in Charentais melon (Cucumis melo var. cantalupensis), AAT are encoded by a gene family of at least four members with amino acid identity ranging from 84% (Cm-AAT1/Cm-AAT2) and 58% (Cm-AAT1/Cm-AAT3) to only 22% (Cm-AAT1/Cm-AAT4). All encoded proteins, except Cm-AAT2, were enzymatically active upon expression in yeast and show differential substrate preferences. Cm-AAT1 protein produces a wide range of short and long-chain acyl esters but has strong preference for the formation of E-2-hexenyl acetate and hexyl hexanoate. Cm-AAT3 also accepts a wide range of substrates but with very strong preference for producing benzyl acetate. Cm-AAT4 is almost exclusively devoted to the formation of acetates, with strong preference for cinnamoyl acetate. Site directed mutagenesis demonstrated that the failure of Cm-AAT2 to produce volatile esters is related to the presence of a 268-alanine residue instead of threonine as in all active AAT proteins. Mutating 268-A into 268-T of Cm-AAT2 restored enzyme activity, while mutating 268-T into 268-A abolished activity of Cm-AAT1. Activities of all three proteins measured with the prefered substrates sharply increase during fruit ripening. The expression of all Cm-AAT genes is up-regulated during ripening and inhibited in antisense ACC oxidase melons and in fruit treated with the ethylene antagonist 1-methylcyclopropene (1-MCP), indicating a positive regulation by ethylene. The data presented in this work suggest that the multiplicity of AAT genes accounts for the great diversity of esters formed in melon.

Indexed as

AcyltransferasesAmino Acid SequenceAmino Acid SubstitutionCucurbitaceaeEstersFruitGene Expression Regulation, EnzymologicGene Expression Regulation, PlantMolecular Sequence DataMultigene FamilyMutagenesis, Site-DirectedMutationPhylogenySequence AlignmentSequence Homology, Amino AcidSubstrate SpecificityAcyltransferasesEstersThreonine

Identifiers

PMID16247561
OpenAlexW2004220904

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.