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Biosynthesis of xylo glucan in suspension cultured soybean glycine max cells evidence that the enzyme system of xylo glucan synthesis does not contain beta 1 4 glucan 4 beta d glucosyl transferase activity ec 2.4.1.12


Biosynthesis of xylo glucan in suspension cultured soybean glycine max cells evidence that the enzyme system of xylo glucan synthesis does not contain beta 1 4 glucan 4 beta d glucosyl transferase activity ec 2.4.1.12



Plant and Cell Physiology 22(8): 1571-1584



ISSN/ISBN: 0032-0781

Xyloglucan 4-.beta.-D-glucosyltransferase, an enzyme responsible for the formation of the xyloglucan backbone, in a particulate preparation of soybean [G. max] cells was compared with .beta.-1,4-glucan 4-.beta.-D-glucosyltransferase of the same origin. Apparently, the enzyme system of xyloglucan synthesis does not contain .beta.-1,4-glucan 4-.beta.-D-glucosyltransferase activity, although both enzymes transfer the glucosyl residue from UDP-glucose to form the .beta.-1,4-glucosidic linkage. The incorporation of [14C]glucose into xyloglucan depended on the presence of UDP-xylose in the incubation mixture. No measurable amount of radioactivity was incorporated from UDP-[14C]xylose into the cello-oligosaccharides, although the incorporation of [14C]xylose into xyloglucan depended on the presence of UDP-glucose in the incubation mixture (Hayashi and Matsuda 1981). The activity of xyloglucan 4-.beta.-D-glucosyltransferase was stimulated more strongly by Mn2+ than by Mg2+; Mg2+ was the most active stimulator for the activity of .beta.-1,4-glucan 4-.beta.-D-glucosyltransferase. An addition of GDP-glucose (100 .mu.M) to the incubation mixture inhibited the activity of xyloglucan 4-.beta.-D-glucosyltransferase by 17%; the activity of .beta.-1,4-glucan 4-.beta.-D-glucosyltransferase was inhibited 56% under the same conditions. Irpex exo-cellulase did not hydrolyze the xyloglucan synthesized in vitro. The .beta.-1,4-glucan synthesized in vitro was not a branched xyloglucan because it gave no 2,3-di-O-methyl glucose derivative on methylation analysis. Pulse-chase experiments indicated that the .beta.-1,4-glucan was not transformed into the xyloglucan. The subcellular distribution of the xyloglucan synthase was similar to that of the .beta.-1,4-glucan synthase (Golgi-located 1,4-.beta.-D-glucan 4-.beta.-D-glucosyltransferase). Apparently, the latter enzyme is located at a site close to xyloglucan synthase and is set aside for the assembly of these polysaccharides into the plant cell surface.

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