Biosynthesis of Methoxypyrazines: Elucidating the Structural/Functional Relationship of Two Vitis vinifera O-Methyltransferases Capable of Catalyzing the Putative Final Step of the Biosynthesis of 3-Alkyl-2-Methoxypyrazine

Jose Vallarino, Xaviera Lopez-Cortes, Jake Dunlevy, Paul Boss, Fernando Gonzalez-Nilo, Yerko Moreno

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    18 Citations (Scopus)

    Abstract

    3-Alkyl-2-methoxypyrazines (MPs) are an important food constituent and have been associated with detrimental herbaceous flavors in red wines by consumers and the wine industry. The Vitis vinifera genes O-methyltransferase 1 and 2 (VvOMT1 and VvOMT2) have been isolated in the grapevine cultivar Carmenere. These genes encode S-adenosyl-l-methionine (SAM)-dependent O-methyltransferases, which have the ability to methylate 3-alkyl-2-hydroxypyrazines (HPs)-the putative final step in MPs production. Atomic studies were performed in order to explain the differences in these VvOMT activities through their structural/functional relationship in MPs biosynthesis. Differences in enthalpy energy observed between the proteins may be due to changes of equivalent residues in the active sites of VvOMT1 (F319, L322) and VvOMT2 (L319, V322). However, docking simulations and QM/MM analyses described how residues H272 and M182 could explain the main functional differentiation observed between VvOMT1 and VvOMT2 through steric impediment, which limits the formation of the transition state in enzymes encoded by VvOMT2. Therefore, this finding could explain the decreasing catalytic efficiency observed for VvOMT2.

    Original languageEnglish
    Pages (from-to)7310-7316
    Number of pages7
    JournalJournal of Agricultural and Food Chemistry
    Volume59
    Issue number13
    DOIs
    Publication statusPublished - 13 Jul 2011

    Keywords

    • docking simulation
    • flavor
    • methoxypyrazines
    • methyltransferases
    • QM/MM
    • Vitis vinifera
    • wine

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