Inhibition of pectin methyl esterase activity by green tea catechins

Kristin C. Lewis, Tzvia Selzer, Chen Shahar, Yael Udi, Dmitry Tworowski, Irit Sagi

Research output: Contribution to journalArticlepeer-review

63 Scopus citations

Abstract

Pectin methyl esterases (PMEs) and their endogenous inhibitors are involved in the regulation of many processes in plant physiology, ranging from tissue growth and fruit ripening to parasitic plant haustorial formation and host invasion. Thus, control of PME activity is critical for enhancing our understanding of plant physiological processes and regulation. Here, we report on the identification of epigallocatechin gallate (EGCG), a green tea component, as a natural inhibitor for pectin methyl esterases. In a gel assay for PME activity, EGCG blocked esterase activity of pure PME as well as PME extracts from citrus and from parasitic plants. Fluorometric tests were used to determine the IC50 for a synthetic substrate. Molecular docking analysis of PME and EGCG suggests close interaction of EGCG with the catalytic cleft of PME. Inhibition of PME by the green tea compound, EGCG, provides the means to study the diverse roles of PMEs in cell wall metabolism and plant development. In addition, this study introduces the use of EGCG as natural product to be used in the food industry and agriculture.

Original languageEnglish
Pages (from-to)2586-2592
Number of pages7
JournalPhytochemistry
Volume69
Issue number14
DOIs
StatePublished - Oct 2008
Externally publishedYes

Funding

We thank Guomin Shan and Bruce D. Hammock, University of California, Davis, for supplying the fluorescent cyano-acetate substrate, Peer Fischer of Rowland Institute at Harvard for fluorometry advice and equipment, Janice Alers-García, Rachel Spicer and Leslie Wright, Rowland Institute at Harvard, for helpful discussion, Jason Figueiredo, Rowland Institute at Harvard for graphics assistance, and Anna Elushin, Weizmann Institute, for technical support. We thank four anonymous reviewers for helpful comments on the manuscript. This work was supported by a Junior Fellowship to K.C.L. from the Rowland Institute at Harvard. I.S. is supported by the Israel Science foundation, the Kimmelman Center at the Weizmann Institute, and the Ambach family fund. I.S. is the incumbent of the Pontecorvo professorial chair.

FundersFunder number
Ambach family fund
Kimmelman Center at the Weizmann Institute
Rowland Institute at Harvard
Israel Science Foundation

    Keywords

    • Camellia sinensis
    • Castilleja indivisa
    • Catechins
    • Cell wall degrading enzymes
    • Cuscuta pentagona
    • Cuscutaceae
    • Dodder
    • Entireleaf Indian paintbrush
    • Epigallocatechin gallate
    • Green tea
    • Inhibition
    • Orobanchaceae
    • Parasitism
    • Pectin methyl esterase
    • Theaceae

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