Effect of L-sorbose on polysaccharide synthetases of Neurospora crassa (glycogen- -1,3-glucan-morphology-cell wall-digitonin-particulate enzymes).

Neurospora glycogen synthetase (EC 2.4.1.11) occurs in 100,000 x g particles. The two forms (glucose-6-phosphate dependent-independent) of glycogen synthetase were solubilized and separated by digitonin treatment of the 100,000 x g particles. Glucan synthetase activity of Neurospora was found only in a cell-wall preparation. These two enzymes have been characterized in relation to the paramorphogenic action of sorbose. Sorbose-grown cultures showed a marked decrease in the specific activity of both enzymes, as compared to sucrose-grown wild-type cultures. Sorbose inhibited the activity of the wild-type enzymes both in vivo and in vitro. In the presence of 5 mM sorbose incorporation of [(14)C]glucose from [(14)C]uridinediphosphate glucose into glycogen by the dependent form of glycogen synthetase was completely inhibited. Thus, the paramorphogenic action of sorbose seems to result from its inhibition of these enzymes of cell-wall biosynthesis. Activities of the enzymes from the sorbose-resistant mutant, patch, were not affected by sorbose either in vivo or in vitro.