ArticleHorticulture research2021
Site-directed mutagenesis identified the key active site residues of alcohol acyltransferase PpAAT1 responsible for aroma biosynthesis in peach fruits.
Article in Horticulture research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 27 citations in OpenAlex.
- Hydrogen sulfide-mediated persulfidation of ERF106 controls pear fruit aroma biosynthesis via disrupting the ERF106-MYB21-FAD8 complex.The Plant journal : for cell and molecular biology · 2026Article
- An Allele of Glutamate Formiminotransferase Triggers 5-Methyl-Tetrahydrofolate-to-MeFox Conversion and Facilitates Folate Biofortification in Maize.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Genome-Wide Identification and Functional Characterization of the BAHD Acyltransferase Gene Family inPlants (Basel, Switzerland) · 2025Article
- Unraveling the trisubstrate-triproduct reaction mechanisms of wine grape VvCYP76F14 to improve wine bouquet.Food chemistry · 2025Article
- D299T Mutation in CYP76F14 Led to a Decrease in Wine Bouquet Precursor Production in Wine Grape.Genes · 2024Article
- Site-Directed Mutagenesis of VvCYP76F14 (Cytochrome P450) Unveils Its Potential for Selection in Wine Grape Varieties Linked to the Development of Wine Bouquet.Journal of agricultural and food chemistry · 2024Article
- Cytochrome P450 VvCYP76F14 dominates the production of wine bouquet precursors in wine grapes.Frontiers in plant science · 2024Article
- Alcohol acyltransferases for the biosynthesis of esters.Biotechnology for biofuels and bioproducts · 2023Review
- Family characteristics, phylogenetic reconstruction, and potential applications of the plant BAHD acyltransferase family.Frontiers in plant science · 2023Review
- Site-directed mutagenesis identified the key active site residues of 2,3-oxidosqualene cyclase HcOSC6 responsible for cucurbitacins biosynthesis inFrontiers in plant science · 2023Article
- Genetic analysis and QTL mapping of aroma volatile compounds in the apple progeny 'Fuji' × 'Cripps Pink'.Frontiers in plant science · 2023Article
- Study on the differences in aroma components and formation mechanisms of "Nasmi" melon from different production areas.Food science & nutrition · 2022Article
- Transcriptomic and Metabolomic Analyses Provide Insights into the Formation of the Peach-like Aroma ofGenes · 2022Article
- Alcohol Acyltransferase Is Involved in the Biosynthesis of C6 Esters in Apricot (Frontiers in plant science · 2021Article
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aroma of peach fruit is predominantly determined by the accumulation of γ-decalactone and ester compounds. A previous study showed that the biosynthesis of these aroma compounds in peach fruit is catalyzed by PpAAT1, an alcohol acyltransferase. In this work, we investigated the key active site residues responsible for γ-decalactone and ester biosynthesis. A total of 14 candidate amino acid residues possibly involved in internal esterification and 9 candidate amino acid residues possibly involved in esterification of PpAAT1 were assessed via site-directed mutagenesis. Analyses of the in vitro enzyme activities of PpAAT1 and its site-directed mutant proteins (PpAAT1-SMs) with different amino acid residue mutations as well as the contents of γ-decalactone in transgenic tobacco leaves and peach fruits transiently expressing PpAAT1 and PpAAT1-SMs revealed that site-directed mutation of H165 in the conserved HxxxD motif led to lost enzymatic activity of PpAAT1 in both internal esterification and its reactions, whereas mutation of the key amino acid residue D376 led to the total loss of γ-decalactone biosynthesis activity of PpAAT1. Mutations of 9 and 7 other amino acid residues also dramatically affected the enzymatic activity of PpAAT1 in the internal esterification and esterification reactions, respectively. Our findings provide a biochemical foundation for the mechanical biosynthesis of γ-decalactone and ester compounds catalyzed by PpAAT1 in peach fruits, which could be used to guide the molecular breeding of new peach species with more favorable aromas for consumers.
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