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Type: Journal article
Title: Plant xyloglucan xyloglucosyl transferases and the cell wall structure: subtle but significant
Author: Stratilova, B.
Kozmon, S.
Stratilova, E.
Hrmova, M.
Citation: Molecules, 2020; 25(23):5619-1-5619-25
Publisher: MDPI
Issue Date: 2020
ISSN: 1420-3049
Statement of
Barbora Stratilová, Stanislav Kozmon, Eva Stratilová and Maria Hrmova
Abstract: Plant xyloglucan xyloglucosyl transferases or xyloglucan endo-transglycosylases (XET; EC catalogued in the glycoside hydrolase family 16 constitute cell wall-modifying enzymes that play a fundamental role in the cell wall expansion and re-modelling. Over the past thirty years, it has been established that XET enzymes catalyse homo-transglycosylation reactions with xyloglucan (XG)-derived substrates and hetero-transglycosylation reactions with neutral and charged donor and acceptor substrates other than XG-derived. This broad specificity in XET isoforms is credited to a high degree of structural and catalytic plasticity that has evolved ubiquitously in algal, moss, fern, basic Angiosperm, monocot, and eudicot enzymes. These XET isoforms constitute gene families that are differentially expressed in tissues in time- and space-dependent manners during plant growth and development, and in response to biotic and abiotic stresses. Here, we discuss the current state of knowledge of broad specific plant XET enzymes and how their inherently carbohydrate-based transglycosylation reactions tightly link with structural diversity that underlies the complexity of plant cell walls and their mechanics. Based on this knowledge, we conclude that multi- or poly-specific XET enzymes are widespread in plants to allow for modifications of the cell wall structure in muro, a feature that implements the multifaceted roles in plant cells.
Keywords: Enzyme structure and function; GH16 family; homo- and hetero-transglycosylation reactions; molecular modelling and simulations; plant cell walls loosening and re-modelling
Rights: © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (
DOI: 10.3390/molecules25235619
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