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

José G. Vallarino, Xaviera A. López-Cortés, Jake D. Dunlevy, Paul K. Boss, Fernando D. González-Nilo, Yerko M. Moreno

Resultado de la investigación: Article

15 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)7310-7316
Número de páginas7
PublicaciónJournal of Agricultural and Food Chemistry
Volumen59
N.º13
DOI
EstadoPublished - 13 jul 2011

Huella dactilar

Wine
Biosynthesis
Vitis
methyltransferases
Methyltransferases
Vitis vinifera
Genes
biosynthesis
wine industry
Flavors
red wines
enthalpy
catalytic activity
active sites
Methionine
methionine
Enthalpy
Catalytic Domain
Industry
genes

ASJC Scopus subject areas

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

Citar esto

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title = "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",
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.",
keywords = "docking simulation, flavor, methoxypyrazines, methyltransferases, QM/MM, Vitis vinifera, wine",
author = "Vallarino, {Jos{\'e} G.} and L{\'o}pez-Cort{\'e}s, {Xaviera A.} and Dunlevy, {Jake D.} and Boss, {Paul K.} and Gonz{\'a}lez-Nilo, {Fernando D.} and Moreno, {Yerko M.}",
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TY - JOUR

T1 - Biosynthesis of methoxypyrazines

T2 - 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

AU - Vallarino, José G.

AU - López-Cortés, Xaviera A.

AU - Dunlevy, Jake D.

AU - Boss, Paul K.

AU - González-Nilo, Fernando D.

AU - Moreno, Yerko M.

PY - 2011/7/13

Y1 - 2011/7/13

N2 - 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.

AB - 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.

KW - docking simulation

KW - flavor

KW - methoxypyrazines

KW - methyltransferases

KW - QM/MM

KW - Vitis vinifera

KW - wine

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