Recognition Properties of Processing α‐Glucosidase I and α‐Glucosidase II

Autor:	Toshiyuki Nishio, Akira Takatsuki, Makoto Muroi, Tadatake Oku, Wataru Hakamata
Rok vydání:	2004
Předmět:	chemistry.chemical_classification Stereochemistry α glucosidase Organic Chemistry Biochemistry chemistry.chemical_compound Hydrolysis Enzyme chemistry Rat liver Phenyl group Moiety Substrate specificity Benzamide
Zdroj:	Journal of Carbohydrate Chemistry. 23:27-39
ISSN:	1532-2327 0732-8303
DOI:	10.1081/car-120030022
Popis:	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‐gluco...
Databáze:	OpenAIRE
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