Plant Xyloglucan Xyloglucosyl Transferases and the Cell Wall Structure: Subtle but Significant.
GH16 family
enzyme structure and function
homo- and hetero-transglycosylation reactions
molecular modelling and simulations
plant cell walls loosening and re-modelling
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
29 Nov 2020
29 Nov 2020
Historique:
received:
25
10
2020
revised:
25
11
2020
accepted:
26
11
2020
entrez:
2
12
2020
pubmed:
3
12
2020
medline:
20
4
2021
Statut:
epublish
Résumé
Plant xyloglucan xyloglucosyl transferases or xyloglucan endo-transglycosylases (XET; EC 2.4.1.207) 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.
Identifiants
pubmed: 33260399
pii: molecules25235619
doi: 10.3390/molecules25235619
pmc: PMC7729885
pii:
doi:
Substances chimiques
Glycosyltransferases
EC 2.4.-
xyloglucan - xyloglucosyltransferase
EC 2.4.1.207
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Australian Research Council
ID : DP120100900
Organisme : VEGA
ID : 2/0137/20
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