Abstract

All four possible monodeoxy derivatives of p‐nitrophenyl α‐D‐glucopyranoside (PNP Glc) and 1‐amino‐2,6‐anhydro‐1‐deoxy‐D‐glycero‐D‐ido‐heptitol derivatives were prepared and used as substrates and inhibitors of rat liver processing α‐glucosidases. α‐Glucosidase II hydrolyzed the 2‐deoxy derivative of PNP Glc (1); the hydrolysis of 1 was more rapid than that of PNP Glc. These results indicate that the presence of a C‐2 hydroxyl group is not essential for the action of α‐glucosidase II. In contrast, PNP Glc and all of the deoxy derivatives of PNP Glc 1–4 inhibited α‐glucosidase I. These results indicate that α‐glucosidase I does not necessarily need all of the hydroxyl groups of the glycon moiety for binding to the enzyme. 2,6‐Anhydro‐1‐benzamide‐D‐glycero‐D‐ido‐heptitol (11), with a terminal phenyl group, inhibited α‐glucosidase I and α‐glucosidase II. Both α‐glucosidase I and II showed the same aglycon specificities. When probes 5–12 were assayed for their ability to inhibit processing by α‐glucosidases at the cellular level, no effects on glycoprotein processing were observed.

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