2,5-Dideoxy-2,5-imino-D-mannitol and -D-glucitol. Two-step bio-organic syntheses from 5-azido-5-deoxy-D-glucofuranose and -L-idofuranose; evaluation as glucosidase inhibitors and application in affinity purification and characterisation of invertase from yeast

Article abstract of DOI:10.1016/0008-6215(93)84155-Y

Glucose isomerase (EC 5.3.1.5) catalyzes the quantitative isomerisation of 5-azido-5-deoxy-D-gluco- (7) and -L-idofuranose (9), respectively, into the corresponding ketoses, 5-azido-5-deoxy-D-fructopyranose (8) and -L-sorbopyranose (10), respectively. Upon catalytic hydrogenation over palladium-on-charcoal, the fructose derivative 8 gives the natural product and the efficient glycosidase inhibitor 2,5-dideoxy-2,5-imino-D-mannitol (4), while the sorbose derivative 10 affords 2,5-dideoxy-2,5-imino-D-glucitol (5). This represents a preparatively very simple and efficient two-step synthesis of these biologically active compounds. Both are strong inhibitors of α- and β-glucosidases from various sources, the D-manno-isomer 4 being distinctly more active. Because of its structural relationship with β-D-fructofuranose, compound 4 is also a vary good inhibitor of invertase from yeast and, as such, was for the first time employed, after immobilized and aminohexyl-sepharose, for the purification of this enzyme. Glucose isomerase (EC 5.3.1.5) catalyses the quantitative isomerization of 5-azido-5-deoxy-D-gluco (7) and -L-idofuranose (9), respectively, into the corresponding ketoses, 5-azido-5-deoxy-D-fructopyranose (8) and -L-sorbopyranose (10) respectively. Upon catalytic hydrogenation over palladium on 2,5-dideoxy-2,5-imino-D-mannitol (4), while the sorbose derivative 10 affords 2,5-dideoxy-2,5-imino-D-glucitol (5). This represents a preparatively very simple and efficient two-step synthesis of these biologically active compounds. Both are strong inhibitors of α- and β-glucosidases from various sources, the D-manno-isomer 4 being distinctly more active. Because of its structural relationship with β-D-fructofuranose, compound 4 is also a very good inhibitor of invertase from yeast and, as such, was for the first time employed, after immobilization on aminohexyl-sepharose, for the purification of this enzyme.