+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Xyloglucan oligosaccharides with at least two alpha-D-xylose residues act as acceptor substrates for xyloglucan endotransglycosylase and promote the depolymerisation of xyloglucan



Xyloglucan oligosaccharides with at least two alpha-D-xylose residues act as acceptor substrates for xyloglucan endotransglycosylase and promote the depolymerisation of xyloglucan



Physiologia Plantarum 88(1): 105-112



A xyloglucan-derived pentasaccharide, Xyl-2 cntdot Glc-3, was shown by viscometry to promote the depolymerisation of xyloglucan by enzyme extracts from bean (Phaseolus vulgaris L. cv. Canadian Wonder) leaves and pea (Pisum sativum L. cv. Alaska) stems. Xyl-2 cntdot Glc-3 was also shown by a radiochemical assay to act as an acceptor substrate for xyloglucan endotransglycosylase activity (XET; EC 2.4.1.-) present in the same extracts. In both these assays, a heptasaccharide (Xyl-3 cntdot Glc-4) was more effective than Xyl-2 cntdot Glc-3 whereas two isomeric tetrasaccharides (Xyl-1 cntdot Glc-3) were essentially ineffective. The agreement in the structural requirements of the two assays suggests that they share a common basis; we therefore propose that the oligosaccharide-sensitive enzyme that depolymerises xyloglucan is XET rather than cellulase (EC 3.2.1.4). In the viscometric assay, the penta- and heptasaccharides would, according to our interpretation, compete with high molecular weight xyloglucan molecules as acceptor substrates for XET, leading to a decrease in the weight-average molecular weight of the xyloglucan and, therefore, to a decrease in viscosity. Our results indicate that oligosaccharides have to possess two alpha-D-xylose residues in order to act as acceptor substrates for XET. The non-reducing end of a high-molecular weight xyloglucan can also act as an acceptor substrate. Therefore, it is likely that exo-hydrolysis by alpha-D-xylosidase would destroy the ability of a polysaccharide to act as an acceptor, even though alpha-D-xylosidase may remove only a single xylose residue from each polysaccharide molecule.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 009739808

Download citation: RISBibTeXText


Related references

Xyloglucan oligosaccharides with at least two a- D-xylose residues act as acceptor substrates for xyloglucan endotransglycosylase and promote the depolymerisation of xyloglucan. Physiologia Plantarum 88: 5-12, 1993

Release of complexed xyloglucan endotransglycosylase (XET) from plant cell walls by a transglycosylation reaction with xyloglucan-derived oligosaccharides. Plant Physiology and Biochemistry 39(11): 927-932, 2001

Kinetic analysis using low-molecular mass xyloglucan oligosaccharides defines the catalytic mechanism of a Populus xyloglucan endotransglycosylase. Biochemical Journal 395(1): 99-106, 2006

Biosynthesis of xyloglucan in suspension-cultured soybean cells. An assay method for xyloglucan xylosyltransferase and attempted synthesis of xyloglucan from UDP-D-xylose. Journal of Biochemistry 89(1): 325-328, 1981

Biosynthesis of Xyloglucan in Suspension-Cultured Soybean Cells. An Assay Method for Xyloglucan Xylosyltransferase and Attempted Synthesis of Xyloglucan from Udp-D-Xylose. The Journal of Biochemistry 89(1): 325-328, 1981

Anionic derivatives of xyloglucan function as acceptor but not donor substrates for xyloglucan endotransglucosylase activity. Planta 227(4): 893-905, 2008

Anionic derivatives of xyloglucan function as acceptor but not donor substrates for xyloglucan endotransglucosylase activity. Planta 227(4): 893-905, 2008

Barley xyloglucan xyloglucosyl transferases bind xyloglucan-derived oligosaccharides in their acceptor-binding regions in multiple conformational states. Archives of Biochemistry and Biophysics 496(1): 61-68, 2010

Functional characterisation of Nicotiana tabacum xyloglucan endotransglycosylase (NtXET-1): generation of transgenic tobacco plants and changes in cell wall xyloglucan. Planta 212(2): 279-287, 2001

Functional characterisation of Nicotiana tabacum xyloglucan endotransglycosylase (NtXet-1): generation of transgenic tobacco plants and changes in cell wall xyloglucan. Planta 212(2): 279-287, 2001

A xyloglucan oligosaccharide specific alpha d xylosidase or exooligoxyloglucan alpha xylohydrolase from germinated nasturtium tropaeolum majus l. seeds purification properties and its interaction with a xyloglucan specific endo 1 4 beta d glucanase and other hydrolases during storage xyloglucan mobilization. Planta (Heidelberg) 184(1): 137-147, 1991

Cleavage of xyloglucan by nasturtium seed xyloglucanase and transglycosylation to xyloglucan subunit oligosaccharides. Archives of Biochemistry and Biophysics 298(2): 365-370, 1992

Xyloglucan oligosaccharides cause cell wall loosening by enhancing xyloglucan endotransglucosylase. Plant and cell physiology 45(1): 77-82, 2004

Biosynthesis of xyloglucan in suspension-cultured soybean cells. Synthesis of xyloglucan from UDP-glucose and UDP-xylose in the cell-free system. Plant and Cell Physiology 22(3): 517-523, 1981

Studies on Production of Fucose-containing Xyloglucan Oligosaccharide. Part Ii. Analysis of the Oligosaccharides of Xyloglucan in Peanut Hulls. Nippon Shokuhin Kagaku Kogaku Kaishi 47(7): 560-563, 2000