| Literature DB >> 16666144 |
T Hayashi1, T Koyama, K Matsuda.
Abstract
Soybean (Glycine max) membranes co-equilibrating with Golgi vesicles in linear sucrose gradients contained UDP-glucuronate carboxy-lyase and xyloglucan synthase activities. Digitonin solubilized and increased the activity of the membrane-bound UDP-glucuronate carboxy-lyase. UDP-xylose did not inhibit the transport of UDP-glucuronate into the lumen of Golgi vesicles but repressed the decarboxylation of the translocated UDP-glucuronate. The results suggest that UDP-glucuronate is transported into the vesicles by a specific carrier and decarboxylated to UDP-xylose within the lumen. On incubation of UDP-[(14)C]glucuronate with Golgi membranes in the presence of UDP-glucose, [(14)C]xylose-labeled xyloglucan was formed. Although the K(m) value of UDP-glucuronate for the decarboxylation was 240 micromolar, the affinity of UDP-glucuronate for xyloglucan formation (31 micromolar) was similar to that of UDP-xylose (28 micromolar), suggesting a high turnover of UDP-xylose. The biosynthesis of UDP-xylose from UDP-glucuronate probably occurs in Golgi membranes, where xyloglucan subsequently forms from UDP-xylose and UDP-glucose.Entities:
Year: 1988 PMID: 16666144 PMCID: PMC1054754 DOI: 10.1104/pp.87.2.341
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340