摘要 : We recently reported that inositol dehydrogenase(EC 1.1.1.18)from Bacillus subtilis can catalyze the highly stereoselective oxidation of 1L-4-O-substituted myo-inositol derivatives,as well as disaccharides melibiose and isomaltose... 展开 We recently reported that inositol dehydrogenase(EC 1.1.1.18)from Bacillus subtilis can catalyze the highly stereoselective oxidation of 1L-4-O-substituted myo-inositol derivatives,as well as disaccharides melibiose and isomaltose,but not gentiobiose or maltose,consistent with the requirement of an alpha-(1->6)linkage.We believed that the enzyme might therefore catalyze efficient stereoselective oxidation of the appropriate alpha-linked glycosyl inositols.We have synthesized alpha-D-glucopyranosyl-(l->4)-(Dh)-myo-inositol and alpha-D-galactopyranosyl-(1->4)-(DL)-myo-inositol using the Appel-Lee protocol to couple benzyl-protected glycosyl donors to protected inositols.This method failed in our hands using glycosyl donors derived from D-mannose and 2-azido-2-deoxy-D-glucose.When myo-inositol 1,3,5-monoorthoformate is used as the acceptor,the reaction is regiospecific for the 4/6-posi-tion.We report here the mildest conditions known for the removal of the orthoformate group.2-Azido-2-deoxy-alpha-D-glucopyrano-syl-(1->4)-(DL)-myo-inositol was synthesized using the trichloroacetimidate derivative as the donor,and all three pseudo-disaccharides were substrates for inositol dehydrogenase.The glucopyranosyl and galactopyranosyl derivatives displayed apparent second-order rate constants comparable to that of myo-inositol. 收起