Trans-α-xylosidase and trans-β-galactosidase activities, widespread in plants, modify and stabilize xyloglucan structures.

The Plant Journal : for Cell and Molecular Biology
Lenka Franková, Stephen C Fry

Abstract

Cell-wall components are hydrolysed by numerous plant glycosidase and glycanase activities. We investigated whether plant enzymes also modify xyloglucan structures by transglycosidase activities. Diverse angiosperm extracts exhibited transglycosidase activities that progressively transferred single sugar residues between xyloglucan heptasaccharide (XXXG or its reduced form, XXXGol) molecules, at 16 μM and above, creating octa- to decasaccharides plus smaller products. We measured remarkably high transglycosylation:hydrolysis ratios under optimized conditions. To identify the transferred monosaccharide(s), we devised a dual-labelling strategy in which a neutral radiolabelled oligosaccharide (donor substrate) reacted with an amino-labelled non-radioactive oligosaccharide (acceptor substrate), generating radioactive cationic products. For example, 37 μM [Xyl-³H]XXXG plus 1 mM XXLG-NH₂ generated ³H-labelled cations, demonstrating xylosyl transfer, which exceeded xylosyl hydrolysis 1.6- to 7.3-fold, implying the presence of enzymes that favour transglycosylation. The transferred xylose residues remained α-linked but were relatively resistant to hydrolysis by plant enzymes. Driselase digestion of the products released a trisaccharide...Continue Reading

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Citations

Apr 23, 2014·Carbohydrate Polymers·Sayani RayMarc Lahaye
Aug 21, 2013·Journal of Experimental Botany·Lenka Franková, Stephen C Fry
Feb 23, 2017·Plant Science : an International Journal of Experimental Plant Biology·Fabienne GuillonMarc Lahaye
Feb 3, 2015·Journal of Integrative Plant Biology·Lenka Franková, Stephen C Fry
Sep 22, 2021·The Plant Journal : for Cell and Molecular Biology·Lenka Franková, Stephen C Fry

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