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  • Substrate specificity of plant and fungi pectin methylesterases: Identification of novel inhibitors of PMEs.

Substrate specificity of plant and fungi pectin methylesterases: Identification of novel inhibitors of PMEs.

International journal of biological macromolecules (2015-09-08)
Mélanie L'Enfant, Jean-Marc Domon, Catherine Rayon, Thierry Desnos, Marie-Christine Ralet, Estelle Bonnin, Jérôme Pelloux, Corinne Pau-Roblot
초록

Pectin methylesterases (PMEs) play a central role in pectin remodeling during plant development. They are also present in phytopathogens such as bacteria and fungi. We investigated the substrate specificity and pH dependence of plant and fungi PMEs using tailor-made pectic substrates. For this purpose, we used two plant PMEs (from orange peel: Citrus sinensis and from Arabidopsis thaliana) and one fungal PME (from Botrytis cinerea). We showed that plant and fungi PMEs differed in their substrate specificity and pH dependence, and that there were some differences between plant PMEs. We further investigated the inhibition of these enzyme activities using characterized polyphenols such as catechins and tannic acid. We showed that PMEs differed in their sensitivity to chemical compounds. In particular, fungal PME was not sensitive to inhibition. Finally, we screened for novel chemical inhibitors of PMEs using a chemical library of ∼3600 compounds. We identified a hundred new inhibitors of plant PMEs, but none had an effect on the fungal enzyme. This study sheds new light on the specificity of pectin methylesterases and provides new tools to modulate their activity.

MATERIALS
제품 번호
브랜드
제품 설명

Sigma-Aldrich
Polyphenon 60 from green tea
Sigma-Aldrich
Alcohol Oxidase solution from Pichia pastoris, buffered aqueous solution, 10-40 units/mg protein (biuret)
Sigma-Aldrich
Pectinesterase from orange peel, lyophilized powder, ≥150 units/mg protein