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donor tamarind xyloglucan + acceptor xyloglucan
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isozymes XTH14 and XTH26 show very high preference for xyloglucan as donor substrate, yet do not work exclusively on xyloglucan, there is a clear preference for the octasaccharide XXLGol, whereas XLLGol is the second best (tested) substrate for isozyme XTH14, it seems a rather poor substrate for isozyme XTH26, which prefers XXFGol
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donor xyloglucan + acceptor xyloglucan
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donor xyloglucan + Xyl(1-6)Glc(1-4)(Xyl(1-6))Glc(1-4)(Fuc-Gal-Xyl(1-6))Glc(1-4)Glc
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?
donor xyloglucan + Xyl(1-6)Glc(1-4)(Xyl(1-6))Glc(1-4)(Fuc-Gal-Xyl(1-6))Glc(1-4)Glc-ol
?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Xylalpha(1-6))Glcbeta(1-4)(Xylalpha(1-6))Glcbeta(1-4)Glc-ol
?
donor xyloglucan + xyloglucan acceptor
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pea xyloglucan
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tamarind xyloglucan
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tamarind xyloglucan + XLLG-9-aminopyrene-1,4,6-trisulfonate
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XET activity assay
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tamarind xyloglucan + XXXG
?
the enzyme performs transglucosylation
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?
tamarind xyloglucan + XXXGol
?
the enzyme performs transglucosylation
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?
XXXG-ol + xyloglucan
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?
XXXGol + xyloglucan
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additional information
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donor xyloglucan + acceptor xyloglucan
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?
donor xyloglucan + acceptor xyloglucan
?
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donor xyloglucan + acceptor xyloglucan
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acceptors: polymer xyloglucan or its derived oligosaccharides
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donor xyloglucan + acceptor xyloglucan
?
acceptor and donor substrate specificities of the isoenzymes TCH4, Meri-5, EXGT and XTR9
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donor xyloglucan + acceptor xyloglucan
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xyloglucan from Tamarindus indica
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donor xyloglucan + acceptor xyloglucan
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donors: TCH4 protein is more active against tamarind xyloglucan than nasturtium xyloglucan as donor, pea stem xyloglucan, acceptors: XLLG-ol, XXFG-ol
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?
donor xyloglucan + acceptor xyloglucan
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isoenzyme XTR9 has a clear preference for non-fucosylated xyloglucan polymers as donor, but not isoenzymes TCH4, Meri-5 and EXGT
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donor xyloglucan + acceptor xyloglucan
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enzyme chooses its donor substrate independently of size and attacks it, once only, at a randomly selected cleavage site
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donor xyloglucan + acceptor xyloglucan
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xyloglucan from Tropaeolum majus seed
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donor xyloglucan + acceptor xyloglucan
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donor specificity
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?
donor xyloglucan + acceptor xyloglucan
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acceptors: xyloglucan oligosaccharide-SR mixture
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?
donor xyloglucan + acceptor xyloglucan
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specific for xyloglucan
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donor xyloglucan + acceptor xyloglucan
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TCH4 protein specifically transglycosylates only xyloglucan, cleavage of both fucosylated and nonfucosylated xyloglucans as donor substrates, but fucosyl content of the substrates lowers reaction rate, preferred acceptor substrate is the nonreducing terminus of high-MW xyloglucan, xyloglucan derived oligosaccharides are also utilized
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donor xyloglucan + Xyl(1-6)Glc(1-4)(Xyl(1-6))Glc(1-4)(Fuc-Gal-Xyl(1-6))Glc(1-4)Glc-ol
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XXFG-ol
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?
donor xyloglucan + Xyl(1-6)Glc(1-4)(Xyl(1-6))Glc(1-4)(Fuc-Gal-Xyl(1-6))Glc(1-4)Glc-ol
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XXFG-ol
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?
donor xyloglucan + Xyl(1-6)Glc(1-4)(Xyl(1-6))Glc(1-4)(Fuc-Gal-Xyl(1-6))Glc(1-4)Glc-ol
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TCH4 protein, 50% as effective as XLLG-ol
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?
donor xyloglucan + Xyl(1-6)Glc(1-4)(Xyl(1-6))Glc(1-4)(Fuc-Gal-Xyl(1-6))Glc(1-4)Glc-ol
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TCH4, Meri-5, EXGT and XTR9 show a marked preference for XLLG-ol over XXFG-ol or XXXG-ol as acceptor oligosaccharide, TCH4, Meri-5 and EXGT: 25-30% as effective as XLLG-ol, less effective than XXXG-ol, XTR9: more effective than XXXG-ol, donor: tamarind or pea xyloglucan polymer
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donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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comparison of the size distributions of the different isoenzymes transglycosylation products
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?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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donor: tamarind xyloglucan
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?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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TCH4, Meri-5, EXGT and XTR9 show a marked preference for XLLG-ol over XXFG-ol or XXXG-ol as acceptor oligosaccharide
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?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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donor: tamarind or pea xyloglucan polymer
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?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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TCH4 protein, better substrate than XXFG-ol, lower affinity than for polymer xyloglucan
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donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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reaction results in a hybrid product and a leaving group
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donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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XLLG-ol
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?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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XLLG-ol
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?
donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Galbeta(1-2)-Xylalpha(1-6))Glcbeta(1-4)(Galbeta(1-2)Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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XLLG-ol
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donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Xylalpha(1-6))Glcbeta(1-4)(Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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TCH4, Meri-5, EXGT and XTR9 show a marked preference for XLLG-ol over XXFG-ol or XXXG-ol as acceptor oligosaccharide, TCH4, Meri-5 and EXGT: more effective than XXFG-ol, XTR9: less effective than XXFG-ol, donor: tamarind or pea xyloglucan polymer
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donor xyloglucan + Xylalpha(1-6)Glcbeta(1-4)(Xylalpha(1-6))Glcbeta(1-4)(Xylalpha(1-6))Glcbeta(1-4)Glc-ol
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XXXG-ol
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donor xyloglucan + xyloglucan acceptor
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Arabidopsis MERI-5 and TCH4 and cauliflower isoenzymes expression occur in dense cytoplasmic tissues predominantly involved in the assembly of new cell walls and thus in the integration of newly secreted xyloglucan into the cell wall
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donor xyloglucan + xyloglucan acceptor
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the xyloglucan:xyloglucosyl transferase gene TCH4 is strongly upregulated by environmental stimuli, enzyme may function in modifying cell walls to allow growth, airspace formation, the development of vasculature, and reinforcement of regions under mechanical strain, TCH4 protein may contribute to the adaptive changes in morphogenesis that occurs in the organism following exposure to mechanical stimuli
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donor xyloglucan + xyloglucan acceptor
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XETs encoded by a gene family may influence plant growth and development, low pH would limit XET function in vivo
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donor xyloglucan + xyloglucan acceptor
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enzyme is unlikely to play a role in acid-induced wall loosening but may function in cold acclimation or cold-tolerant growth, TCH4 expression is rapidly regulated by mechanical stimuli, temperature shifts, light and hormones, it may be involved in assembling nascent cell walls or reinforcing existing and expanding walls
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donor xyloglucan + xyloglucan acceptor
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acts in root development, necessary for root hair growth
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donor xyloglucan + xyloglucan acceptor
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existence of different classes of XET with differing roles in vivo
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donor xyloglucan + xyloglucan acceptor
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role in cell elongation
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donor xyloglucan + xyloglucan acceptor
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enzyme is capable of splitting and reconnecting xyloglucan molecules in rapidly growing plant tissues, expression and presumed physiological roles of At-XTH22 and 24
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donor xyloglucan + xyloglucan acceptor
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Arabidopsis EXGT and mung bean isoenzymes expression in tissues involved in the loosening of existing cell wall material necessary for rapid cell expansion, e.g. vacuolation
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
?
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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additional information
?
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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?
additional information
?
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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?
additional information
?
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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?
additional information
?
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not: cellobiose-SR
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?
additional information
?
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not: carboxymethylcellulose, barley glucan
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?
additional information
?
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contains strongly conserved sequence motif of XETs: DEIDFEFLG
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?
additional information
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contains strongly conserved sequence motif of XETs: DEIDFEFLG
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?
additional information
?
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no endoglucanase activity
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?
additional information
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no endoglucanase activity
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?
additional information
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free oligosaccharides are probably not the usual acceptor substrates in vivo
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?
additional information
?
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breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan
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?
additional information
?
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breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan
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?
additional information
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anionic, oxidised derivatives of xyloglucan are used as substrates for AtXTH24
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additional information
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isozyme XTH14 uses donor substrates in order of preference xyloglucan >> watersoluble cellulose acetate > hydroxyethylcellulose > mixed-linkage beta-glucan > carboxymethylcellulose > methylcellulose, thus, all nonxyloglucan substrates show very low activity rates in comparison to xyloglucan. Isozyme XTH26 is able to use watersoluble cellulose acetate at a low rate but shows no activity with any of the other non-xyloglucan substrates tested
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview. AtXTH13 catalyzes the release of XGO1 (Glc4-based xylogluco-oligosaccharides) and XGO3 (Glc12-based xyloglucooligosaccharides) from a mixture of minimal XET/XEH substrates, XGO2 (Glc8-based xylogluco-oligosaccharides), derived from tamarind seed xyloglucan and bearing naturally variable galactosylation. The rate of release of XGO1 is identical to that of XGO3 at all substrate concentrations across a wide range
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview. AtXTH13 catalyzes the release of XGO1 (Glc4-based xylogluco-oligosaccharides) and XGO3 (Glc12-based xyloglucooligosaccharides) from a mixture of minimal XET/XEH substrates, XGO2 (Glc8-based xylogluco-oligosaccharides), derived from tamarind seed xyloglucan and bearing naturally variable galactosylation. The rate of release of XGO1 is identical to that of XGO3 at all substrate concentrations across a wide range
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview. AtXTH13 catalyzes the release of XGO1 (Glc4-based xylogluco-oligosaccharides) and XGO3 (Glc12-based xyloglucooligosaccharides) from a mixture of minimal XET/XEH substrates, XGO2 (Glc8-based xylogluco-oligosaccharides), derived from tamarind seed xyloglucan and bearing naturally variable galactosylation. The rate of release of XGO1 is identical to that of XGO3 at all substrate concentrations across a wide range
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview. AtXTH13 catalyzes the release of XGO1 (Glc4-based xylogluco-oligosaccharides) and XGO3 (Glc12-based xyloglucooligosaccharides) from a mixture of minimal XET/XEH substrates, XGO2 (Glc8-based xylogluco-oligosaccharides), derived from tamarind seed xyloglucan and bearing naturally variable galactosylation. The rate of release of XGO1 is identical to that of XGO3 at all substrate concentrations across a wide range
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additional information
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview. AtXTH13 catalyzes the release of XGO1 (Glc4-based xylogluco-oligosaccharides) and XGO3 (Glc12-based xyloglucooligosaccharides) from a mixture of minimal XET/XEH substrates, XGO2 (Glc8-based xylogluco-oligosaccharides), derived from tamarind seed xyloglucan and bearing naturally variable galactosylation. The rate of release of XGO1 is identical to that of XGO3 at all substrate concentrations across a wide range
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additional information
?
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XTH isozyme spcificities with different donor substrates, tamarind xyloglucan-derived oligosacchrides, overview. AtXTH13 catalyzes the release of XGO1 (Glc4-based xylogluco-oligosaccharides) and XGO3 (Glc12-based xyloglucooligosaccharides) from a mixture of minimal XET/XEH substrates, XGO2 (Glc8-based xylogluco-oligosaccharides), derived from tamarind seed xyloglucan and bearing naturally variable galactosylation. The rate of release of XGO1 is identical to that of XGO3 at all substrate concentrations across a wide range
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additional information
?
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XTH isozyme specificity with different donor substrates, tamarind xyloglucan-derived oligosaccharides, overview
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additional information
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XTH isozyme specificity with different donor substrates, tamarind xyloglucan-derived oligosaccharides, overview
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additional information
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XTH isozyme specificity with different donor substrates, tamarind xyloglucan-derived oligosaccharides, overview
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additional information
?
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XTH isozyme specificity with different donor substrates, tamarind xyloglucan-derived oligosaccharides, overview
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additional information
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XTH isozyme specificity with different donor substrates, tamarind xyloglucan-derived oligosaccharides, overview
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additional information
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XTH isozyme specificity with different donor substrates, tamarind xyloglucan-derived oligosaccharides, overview
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additional information
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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additional information
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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additional information
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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additional information
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enzyme activity assay with partially purified tamarind xyloglucan as donor and [3H]XXXG-ol as xyloglucan acceptor substrate
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additional information
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isozyme XHT31 shows predominant undetectable xyloglucan endohydrolase, XEH, activity and has only slight xyloglucan endotransglucosylase, XET, activity in vitro. Usage of XXXG-ol as acceptor substrate and of xyloglucan as donor substrate. XXXG-ol is the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested. Isozyme XTH31's XET activity is strongly compromised when the second Xyl residue is galactosylated. XTH31 cleaves the substrate from about 186 kDa to 6 kDa (median sizes) within 40 h, gas spectrometric analysis. The isozyme does not have a preferred cleavage site close to either terminus. The complete hydrolysis of a 186-kDa tamarind xyloglucan molecule to yield Glc4-based oligosaccharides would require about 150 cuts. XEH action continues for at least 40 h, with an initial rate of about 1.5 cuts per starting molecule per hour. Substrate specificity of Arabidopsis thaliana XET isozymes XTH15 and XTH31, overview. The acceptor site of XTH31 is relatively poor at accommodating substrates that have Gal (or Fuc-Gal) simultaneously on the 2nd and 3rd isoprimeverose groups, counted from the nonreducing end
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additional information
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isozyme XHT31 shows predominant undetectable xyloglucan endohydrolase, XEH, activity and has only slight xyloglucan endotransglucosylase, XET, activity in vitro. Usage of XXXG-ol as acceptor substrate and of xyloglucan as donor substrate. XXXG-ol is the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested. Isozyme XTH31's XET activity is strongly compromised when the second Xyl residue is galactosylated. XTH31 cleaves the substrate from about 186 kDa to 6 kDa (median sizes) within 40 h, gas spectrometric analysis. The isozyme does not have a preferred cleavage site close to either terminus. The complete hydrolysis of a 186-kDa tamarind xyloglucan molecule to yield Glc4-based oligosaccharides would require about 150 cuts. XEH action continues for at least 40 h, with an initial rate of about 1.5 cuts per starting molecule per hour. Substrate specificity of Arabidopsis thaliana XET isozymes XTH15 and XTH31, overview. The acceptor site of XTH31 is relatively poor at accommodating substrates that have Gal (or Fuc-Gal) simultaneously on the 2nd and 3rd isoprimeverose groups, counted from the nonreducing end
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additional information
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isozyme XHT31 shows predominant undetectable xyloglucan endohydrolase, XEH, activity and has only slight xyloglucan endotransglucosylase, XET, activity in vitro. Usage of XXXG-ol as acceptor substrate and of xyloglucan as donor substrate. XXXG-ol is the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested. Isozyme XTH31's XET activity is strongly compromised when the second Xyl residue is galactosylated. XTH31 cleaves the substrate from about 186 kDa to 6 kDa (median sizes) within 40 h, gas spectrometric analysis. The isozyme does not have a preferred cleavage site close to either terminus. The complete hydrolysis of a 186-kDa tamarind xyloglucan molecule to yield Glc4-based oligosaccharides would require about 150 cuts. XEH action continues for at least 40 h, with an initial rate of about 1.5 cuts per starting molecule per hour. Substrate specificity of Arabidopsis thaliana XET isozymes XTH15 and XTH31, overview. The acceptor site of XTH31 is relatively poor at accommodating substrates that have Gal (or Fuc-Gal) simultaneously on the 2nd and 3rd isoprimeverose groups, counted from the nonreducing end
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additional information
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isozyme XTH15 has high xyloglucan endotransglucosylase, XET, and undetectable xyloglucan endohydrolase, XEH, activity in vitro. Usage of XXXG-ol as acceptor substrate and of xyloglucan as donor substrate. XXXG-ol is the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested. XTH15's XET activity tolerateds substitution at the second Xyl residue. Substrate specificity of Arabidopsis thaliana XET isozymes XTH15 and XTH31, overview
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additional information
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isozyme XTH15 has high xyloglucan endotransglucosylase, XET, and undetectable xyloglucan endohydrolase, XEH, activity in vitro. Usage of XXXG-ol as acceptor substrate and of xyloglucan as donor substrate. XXXG-ol is the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested. XTH15's XET activity tolerateds substitution at the second Xyl residue. Substrate specificity of Arabidopsis thaliana XET isozymes XTH15 and XTH31, overview
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additional information
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isozyme XTH15 has high xyloglucan endotransglucosylase, XET, and undetectable xyloglucan endohydrolase, XEH, activity in vitro. Usage of XXXG-ol as acceptor substrate and of xyloglucan as donor substrate. XXXG-ol is the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested. XTH15's XET activity tolerateds substitution at the second Xyl residue. Substrate specificity of Arabidopsis thaliana XET isozymes XTH15 and XTH31, overview
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additional information
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enzyme XTH15, a classical group-I/II xyloglucan endotransglucosylase/hydrolase (XTH), has high xyloglucan endotransglucosylase (XET) and undetectable xyloglucan hydrolase (XEH) activity in vitro
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additional information
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enzyme XTH15, a classical group-I/II xyloglucan endotransglucosylase/hydrolase (XTH), has high xyloglucan endotransglucosylase (XET) and undetectable xyloglucan hydrolase (XEH) activity in vitro
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additional information
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evaluation of the substrate specificities of xyloglucan acceptors by using a set of synthetic oligosaccharides obtained by automated glycan assembly. The ability of XETs to incorporate the oligosaccharides into polysaccharides printed as microarrays and into stem sections is assessed, showing that single xylose substitutions are sufficient for transfer, and xylosylation of the terminal glucose residue is not required by XETs, independent of plant species. To obtain information on the potential xylosylation pattern of the natural acceptor of XETs, that is, the nonreducing end of xyloglucan, the activity of xyloglucan xylosyl transferase (XXT) 2 on the synthetic xyloglucan oligosaccharides is tested. Acceptor substrate specificities of XET, overview
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additional information
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[3H]XXXGol and tamarind xyloglucan are used as substrates in a radioactive enzyme assay to yield [3H]polysaccharide
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donor xyloglucan + acceptor xyloglucan
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donor xyloglucan + xyloglucan acceptor
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additional information
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donor xyloglucan + xyloglucan acceptor
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Arabidopsis MERI-5 and TCH4 and cauliflower isoenzymes expression occur in dense cytoplasmic tissues predominantly involved in the assembly of new cell walls and thus in the integration of newly secreted xyloglucan into the cell wall
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donor xyloglucan + xyloglucan acceptor
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the xyloglucan:xyloglucosyl transferase gene TCH4 is strongly upregulated by environmental stimuli, enzyme may function in modifying cell walls to allow growth, airspace formation, the development of vasculature, and reinforcement of regions under mechanical strain, TCH4 protein may contribute to the adaptive changes in morphogenesis that occurs in the organism following exposure to mechanical stimuli
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donor xyloglucan + xyloglucan acceptor
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XETs encoded by a gene family may influence plant growth and development, low pH would limit XET function in vivo
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donor xyloglucan + xyloglucan acceptor
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enzyme is unlikely to play a role in acid-induced wall loosening but may function in cold acclimation or cold-tolerant growth, TCH4 expression is rapidly regulated by mechanical stimuli, temperature shifts, light and hormones, it may be involved in assembling nascent cell walls or reinforcing existing and expanding walls
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donor xyloglucan + xyloglucan acceptor
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acts in root development, necessary for root hair growth
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donor xyloglucan + xyloglucan acceptor
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existence of different classes of XET with differing roles in vivo
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donor xyloglucan + xyloglucan acceptor
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role in cell elongation
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donor xyloglucan + xyloglucan acceptor
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enzyme is capable of splitting and reconnecting xyloglucan molecules in rapidly growing plant tissues, expression and presumed physiological roles of At-XTH22 and 24
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donor xyloglucan + xyloglucan acceptor
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Arabidopsis EXGT and mung bean isoenzymes expression in tissues involved in the loosening of existing cell wall material necessary for rapid cell expansion, e.g. vacuolation
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH19 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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free oligosaccharides are probably not the usual acceptor substrates in vivo
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additional information
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breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan
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additional information
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breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH1 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH13 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. The endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH17 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
-
root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
additional information
?
-
root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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additional information
?
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root-specific isozyme AtXTH18 exhibits only the endotransglucosylase activity, XET, EC 2.4.1.207, towards xyloglucan and non-detectable endohydrolytic activity, XEH, EC 3.2.1.151. Its endotransglucosylase activity is preferentially directed towards xyloglucan and water-soluble cellulose acetate, rather than to mixed-linkage beta-glucan
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?
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metabolism
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the plant cell wall is a cellular exoskeleton consisting predominantly of a complex polysaccharide network that defines the shape of cells. During growth, this network can be loosened through the action of xyloglucan endotransglycosylases (XETs), glycoside hydrolases that cut and paste xyloglucan polysaccharides through a transglycosylation process
physiological function
xyloglucan endotransglucosylase/hydrolases are cell wall enzymes that are able to graft xyloglucan chains to oligosaccharides or to other available xyloglucan chains and/or to hydrolyse xyloglucan chains. As they are involved in the modification of the load-bearing cell-wall components, they are believed to be very important in the regulation of growth and development
physiological function
the primary cell wall of flowering plants consists of cellulose fibrils tethered by hemicelluloses (principally xyloglucans) and embedded in an amorphous matrix of pectins and glycoproteins. Plant cell expansion is mainly regulated by cell wall extensibility and results from selective loosening and rearrangement of the load-bearing cellulose/xyloglucan network, at least in flowering plants with type I cell walls where xyloglucan is a predominant hemicellulose. Xyloglucan endotransglucosylase/hydrolases (XTHs), a class of cell wall-modifying proteins, also have the capacity to loosen cell walls. Most XTHs cut and rejoin xyloglucan by xyloglucan endotransglucosylase, EC 2.4.1.207, action, whereas some XTHs hydrolyse xyloglucan by xyloglucan hydrolase, XEH EC 3.2.1.151, action
evolution
xyloglucan endotransglucosylase/hydrolases (XTHs) are encoded in Arabidopsis by a 33-member gene family, isozyme XTH15 is a classical group-I/II XTH
evolution
xyloglucan endotransglucosylase/hydrolases (XTHs) are encoded in Arabidopsis by a 33-member gene family, isozyme XTH31 is a group-III-A XTH
malfunction
mutant seedlings defective in XTH15 exhibit no visible growth defects possibly because isozyme XTH16 closely resembles XTH15 in sequence, pI and expression profile
malfunction
loss-of-function of XTH30 leads to increased salt tolerance and overexpression of XTH30 results in salt hypersensitivity. Loss-of-function of XTH30 slows down the decrease of crystalline cellulose content and the depolymerization of microtubules caused by salt stress. Lower Na+ accumulation in shoot and lower H2O2 content are found in xth30 mutants in response to salt stress. The xth30 mutants wilt less and show a much higher survival rate than the wild-type under 125 mM NaCl treatment. XTH30 affects the xyloglucan oligosaccharide composition during salt stress
physiological function
XTH28 is specifically involved in the growth of stamen fi laments, and is required for successful automatic self-pollination in certain flowers in Arabidopsis thaliana
physiological function
xyloglucan endotransglucosylase/hydrolases are cell wall enzymes that are able to graft xyloglucan chains to oligosaccharides or to other available xyloglucan chains and/or to hydrolyse xyloglucan chains. As they are involved in the modification of the load-bearing cell-wall components, they are believed to be very important in the regulation of growth and development
physiological function
xyloglucan endotransglucosylase/hydrolases are cell wall enzymes that are able to graft xyloglucan chains to oligosaccharides or to other available xyloglucan chains and/or to hydrolyse xyloglucan chains. As they are involved in the modification of the load-bearing cell-wall components, they are believed to be very important in the regulation of growth and development. AtXTH13 might play a role later in root hair development
physiological function
xyloglucan endotransglucosylase/hydrolases are cell wall enzymes that are able to graft xyloglucan chains to oligosaccharides or to other available xyloglucan chains and/or to hydrolyse xyloglucan chains. As they are involved in the modification of the load-bearing cell-wall components, they are believed to be very important in the regulation of growth and development. Role for AtXTH12 in root hair initiation. AtXTH13 might play a role later in root hair development
physiological function
isozyme XTH15 is predominantly expressed in early-stage organs, and thus seem likely to participate in cell expansion
physiological function
isozyme XTH31 is predominantly expressed in early-stage organs, and thus seem likely to participate in cell expansion. XTH31 is responsible for a specific mode of cell elongation that is particularly Al3+-sensitive. In the wild-type, a second mode of cell expansion that is more Al3+-resistant must be occurring simultaneously
physiological function
the primary cell wall of flowering plants consists of cellulose fibrils tethered by hemicelluloses (principally xyloglucans) and embedded in an amorphous matrix of pectins and glycoproteins. Plant cell expansion is mainly regulated by cell wall extensibility and results from selective loosening and rearrangement of the load-bearing cellulose/xyloglucan network, at least in flowering plants with type I cell walls where xyloglucan is a predominant hemicellulose. Xyloglucan endotransglucosylase/hydrolases (XTHs), a class of cell wall-modifying proteins, also have the capacity to loosen cell walls. Most XTHs cut and rejoin xyloglucan by xyloglucan endotransglucosylase, EC 2.4.1.207, action, whereas some XTHs hydrolyse xyloglucan by xyloglucan hydrolase, XEH EC 3.2.1.151, action
physiological function
the primary cell wall of flowering plants consists of cellulose fibrils tethered by hemicelluloses (principally xyloglucans) and embedded in an amorphous matrix of pectins and glycoproteins. Plant cell expansion is mainly regulated by cell wall extensibility and results from selective loosening and rearrangement of the load-bearing cellulose/xyloglucan network, at least in flowering plants with type I cell walls where xyloglucan is a predominantchemicellulose. Xyloglucan endotransglucosylase/hydrolases (XTHs), a class of cell wall-modifying proteins, also have the capacity to loosen cell walls. Most XTHs cut and rejoin xyloglucan by xyloglucan endotransglucosylase, EC 2.4.1.207, action, whereas some XTHs hydrolyse xyloglucan by xyloglucan hydrolase, XEH EC 3.2.1.151, action
physiological function
a role for enzyme XTH31 in acid growth. Isozymes XTH15 and XTH31 are both strongly expressed in young, rapidly growing organs, suggesting that they play roles in cell expansion. In vitro, XTH15 has very high transglucanase (endotransglucosylase, XET) but undetectable hydrolytic activity (glucanase, XEH). In contrast, XTH31 has very high XEH activity and only slight XET activity
physiological function
isozymes XTH15 and XTH31 are both strongly expressed in young, rapidly growing organs, suggesting that they play roles in cell expansion. In vitro, XTH15 has very high transglucanase (endotransglucosylase, XET) but undetectable hydrolytic activity (glucanase, XEH). In contrast, XTH31 has very high XEH activity and only slight XET activity
physiological function
xyloglucan endotransglucosylase (XET) activity, which cuts and re-joins hemicellulose chains in the plant cell wall, contributing to wall assembly and growth regulation, is the major activity of XTH proteins. During purification, XTHs often lose XET activity which, however, is restored by treatment with certain cold-water-extractable, heat-stable polymers (CHPs), e.g. from cauliflower florets
physiological function
-
the plant cell wall is a cellular exoskeleton consisting predominantly of a complex polysaccharide network that defines the shape of cells. During growth, this network can be loosened through the action of xyloglucan endotransglycosylases (XETs), glycoside hydrolases that cut and paste xyloglucan polysaccharides through a transglycosylation process
physiological function
xyloglucan (XyG) is an important hemicellulose polymer of the primary cell wall in dicotyledons and non-commelinid monocotyledons. XyG plays a vital role in loosening or stiffening the cell wall by binding to cellulose microfibrils with hydrogen bonds during cell elongation. XyG chains can be cleaved or rejoined by xyloglucan endotransglucosylase-hydrolase (XTH). Alteration to the cell wall is one strategy that helps plants adapt to salt stress. Isozyme xyloglucan endotransglucosylase-hydrolase 30 (XTH30) negatively affects salt tolerance in Arabidopsis thaliana. XTH30 modulates XyG side chains, alters abundance of XLFG, cellulose synthesis, and cortical microtubule stability, and negatively affects salt tolerance. And XTH30 aggravates depolymerization of cortical microtubules under salt stress
additional information
XTHs in dilute solution bind to diverse surfaces (e.g. glass and cellulose), and certain cold-water-extractable, heat-stable polymers (CHPs), e.g. from cauliflower florets, can re-solubilise the bound enzyme, re-activating it. Cell walls prepared from cauliflower florets, mung bean shoots and Arabidopsis cell-suspension cultures each contain endogenous, tightly bound, inactive XTHs, which are likewise rapidly solubilised and thus activated by cauliflower XTH-activating factor (XAF). Analysis of XTH-activating factor (XAF) activity of CHP preparations from diverse plant sources, CHPs from all plants tested possess XAF activity, overview
additional information
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XTHs have a tendency to bind to various surfaces, including chromatography columns and cellulose. Bovine serum albumin (BSA) minimizes binding of solubilized XTHs to tube walls. BSA is the only agent which leads to the measured XET activity being proportional to the concentration of added enzyme: in all three types of plastic, reducing the concentration of the crude enzyme solution from 50% v/v to 15% v/v decrease the measured XET reaction rate by about 70%. Therefore, BSA at 2.5 mg/mL is included in the reaction mixture used in all subsequent XET assays
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Purugganan, M.M.; Braam, J.; Fry, S.C.
The Arabidopsis TCH4 xyloglucan endotransglycosylase. Substrate specificity, pH optimum, and cold tolerance
Plant Physiol.
115
181-190
1997
Arabidopsis thaliana
brenda
Antosiesicz, D.M.; Purugganan, M.M.; Polisensky, D.H.; Braam, J.
Cellular localization of Arabidopsis xyloglucan endotransglycosylase-related proteins during development and after wind stimulation
Plant Physiol.
115
1319-1328
1997
Arabidopsis thaliana
brenda
Steele, N.M.; Sulova, Z.; Campbell, P.; Braam, J.; Farkas, V.; Fry, S.C.
Ten isoenzymes of xyloglucan endotransglycosylase from plant cell walls select and cleave the donor substrate stochastically
Biochem. J.
355
671-679
2001
Arabidopsis thaliana, Brassica oleracea, Lens culinaris, Vigna radiata var. radiata, Tropaeolum majus
brenda
Campbell, P.; Braam, J.
In vitro activities of four xyloglucan endotransglycosylases from Arabidopsis
Plant J.
18
371-382
1999
Arabidopsis thaliana, Arabidopsis thaliana (Q9ZSU4)
brenda
Rose, J.K.C.; Braam, J.; Fry, S.C.; Nishitani, K.
The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: Current perspectives and a new unifying nomenclature
Plant Cell Physiol.
43
1421-1435
2002
Apium sp., Arabidopsis thaliana, Solanum lycopersicum, Nicotiana tabacum, Vigna angularis, Pisum sativum, Spinacia oleracea, Tropaeolum majus
brenda
Vissenberg, K.; Van Sandt, V.; Fry, S.C.; Verbelen, J.P.
Xyloglucan endotransglucosylase action is high in the root elongation zone and in the trichoblasts of all vascular plants from Selaginella to Zea mays
J. Exp. Bot.
54
335-344
2003
Adiantum capillus-veneri, Aloe sp., Anthurium upalaense, Anthurium willdenowii, Arabidopsis thaliana, Asphodelus fistulosus, Azolla sp., Beckmannia syzigachne, Blumenbachia hieronymi, Briza maxima, Cistanthe grandiflora, Callistephus chinensis, Canna indica, Carex flacca, Cedrus atlantica, Cenchrus ciliaris, Chaenorhinum minus, Chamaecyparis sp., Chamaecyparis thyoides, Chamaedorea elegans, Centaurea benedicta, Cochlearia officinalis, Commelina nilagirica, Convallaria majalis, Crocus vernus, Cyperus prolifer, Dracaena draco, Elsholtzia ciliata, Euphorbia helioscopia, Helianthus annuus, Ipomoea purpurea, Iris pseudacorus, Juncus effusus, Lactuca perennis, Lemna minor, Linum usitatissimum, Luzula luzuloides, Leptochilus pteropus, Musa x paradisiaca, Nicotiana tabacum, Peperomia rotundifolia, Picea abies, Pinus parviflora, Pinus radiata, Pitcairnia imbricata, Pothomorphe petalta, Pteris cretica, Scabiosa atropurpurea, Selaginella sp., Taxus baccata, Tradescantia zebrina, Tragopodon pratensis, Trigonella caerulea, Triticum dicoccum, Typha angustifolia, Typha latifolia, Festuca myuros, Zea mays, Pinus parviflora Glauca, Ipomoea purpurea Bojer, Trigonella caerulea Ser., Beckmannia syzigachne Fernald, Nicotiana tabacum SR-1, Cedrus atlantica Carr., Crocus vernus Hill
brenda
Divol, F.; Vilaine, F.; Thibivilliers, S.; Kusiak, C.; Sauge, M.H.; Dinant, S.
Involvement of the xyloglucan endotransglycosylase/hydrolases encoded by celery XTH1 and Arabidopsis XTH33 in the phloem response to aphids
Plant Cell Environ.
30
187-201
2007
Apium graveolens, Arabidopsis thaliana
brenda
Vissenberg, K.; Oyama, M.; Osato, Y.; Yokoyama, R.; Verbelen, J.P.; Nishitani, K.
Differential expression of AtXTH17, AtXTH18, AtXTH19 and AtXTH20 genes in Arabidopsis roots. Physiological roles in specification in cell wall construction
Plant Cell Physiol.
46
192-200
2005
Arabidopsis thaliana
brenda
Liu, Y.B.; Lu, S.M.; Zhang, J.F.; Liu, S.; Lu, Y.T.
A xyloglucan endotransglucosylase/hydrolase involves in growth of primary root and alters the deposition of cellulose in Arabidopsis
Planta
226
1547-1560
2007
Arabidopsis thaliana (Q9ZV40), Arabidopsis thaliana
brenda
Takeda, T.; Miller, J.G.; Fry, S.C.
Anionic derivatives of xyloglucan function as acceptor but not donor substrates for xyloglucan endotransglucosylase activity
Planta
227
893-905
2008
Arabidopsis thaliana (P24806)
brenda
Kurasawa, K.; Matsui, A.; Yokoyama, R.; Kuriyama, T.; Yoshizumi, T.; Matsui, M.; Suwabe, K.; Watanabe, M.; Nishitani, K.
The AtXTH28 gene, a xyloglucan endotransglucosylase/hydrolase, is involved in automatic self-pollination in Arabidopsis thaliana
Plant Cell Physiol.
50
413-422
2009
Arabidopsis thaliana (Q38909), Arabidopsis thaliana
brenda
Maris, A.; Suslov, D.; Fry, S.C.; Verbelen, J.P.; Vissenberg, K.
Enzymic characterization of two recombinant xyloglucan endotransglucosylase/hydrolase (XTH) proteins of Arabidopsis and their effect on root growth and cell wall extension
J. Exp. Bot.
60
3959-3972
2009
Arabidopsis thaliana
brenda
Maris, A.; Kaewthai, N.; Ekloef, J.M.; Miller, J.G.; Brumer, H.; Fry, S.C.; Verbelen, J.P.; Vissenberg, K.
Differences in enzymic properties of five recombinant xyloglucan endotransglucosylase/hydrolase (XTH) proteins of Arabidopsis thaliana
J. Exp. Bot.
62
261-271
2011
Arabidopsis thaliana (O80803), Arabidopsis thaliana (Q9FKL8), Arabidopsis thaliana (Q9FKL9), Arabidopsis thaliana (Q9M0D1), Arabidopsis thaliana (Q9M0D2), Arabidopsis thaliana
brenda
Miedes, E.; Suslov, D.; Vandenbussche, F.; Kenobi, K.; Ivakov, A.; Van Der Straeten, D.; Lorences, E.P.; Mellerowicz, E.J.; Verbelen, J.P.; Vissenberg, K.
Xyloglucan endotransglucosylase/hydrolase (XTH) overexpression affects growth and cell wall mechanics in etiolated Arabidopsis hypocotyls
J. Exp. Bot.
64
2481-2497
2013
Populus tremula x Populus tremuloides (Q8GZD5), Arabidopsis thaliana (Q9FI31), Arabidopsis thaliana (Q9M0D1), Arabidopsis thaliana (Q9M0D2), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9FI31), Arabidopsis thaliana Col-0 (Q9M0D1), Arabidopsis thaliana Col-0 (Q9M0D2)
brenda
Shi, Y.Z.; Zhu, X.F.; Miller, J.G.; Gregson, T.; Zheng, S.J.; Fry, S.C.
Distinct catalytic capacities of two aluminium-repressed Arabidopsis thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31, heterologously produced in Pichia
Phytochemistry
112
160-169
2015
no activity in Pichia pastoris, Arabidopsis thaliana (P93046), Arabidopsis thaliana (Q38911), Arabidopsis thaliana
brenda
Sharples, S.C.; Nguyen-Phan, T.C.; Fry, S.C.
Xyloglucan endotransglucosylase/hydrolases (XTHs) are inactivated by binding to glass and cellulosic surfaces, and released in active form by a heat-stable polymer from cauliflower florets
J. Plant Physiol.
218
135-143
2017
Arabidopsis thaliana (P24806), Vigna radiata (Q5MB21), Brassica oleracea var. botrytis (Q6YDN9), Brassica oleracea var. botrytis
brenda
Shi, Y.; Zhu, X.; Miller, J.; Gregson, T.; Zheng, S.; Fry, S.
Distinct catalytic capacities of two aluminium-repressed Arabidopsis thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31, heterologously produced in Pichia
Phytochemistry
112
160-169
2015
no activity in Pichia pastoris, Arabidopsis thaliana (P93046), Arabidopsis thaliana (Q38911)
-
brenda
Nguyen-Phan, T.C.; Fry, S.C.
Functional and chemical characterization of XAF a heat-stable plant polymer that activates xyloglucan endotransglucosylase/hydrolase (XTH)
Ann. Bot.
124
131-148
2019
Arabidopsis thaliana
brenda
Ruprecht, C.; Dallabernardina, P.; Smith, P.; Urbanowicz, B.; Pfrengle, F.
Analyzing xyloglucan endotransglycosylases by incorporating synthetic oligosaccharides into plant cell walls
ChemBioChem
19
793-798
2018
Arabidopsis thaliana, Pisum sativum (Q9FXQ4)
brenda
Yan, J.; Huang, Y.; He, H.; Han, T.; Di, P.; Sechet, J.; Fang, L.; Liang, Y.; Scheller, H.; Mortimer, J.; Ni, L.; Jiang, M.; Hou, X.; Zhang, A.; Zhang, J.
Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis
J. Exp. Bot.
70
5495-5506
2019
Arabidopsis thaliana (Q38908), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q38908)
brenda