a-Glucosidases are among the most important carbohydrate-splitting enzymes. They catalyze the hydrolysis of a-glucosidic linkages. Their substrates are-depending on their specificity-oligo-and polysaccharides. Microbial inhibitors of a-amylases and other mammalian intestinal carbohydrate-splitting enzymes studied during the last few years have aroused medical interest in the treatment of metabolic diseases such as diabetes. Moreover, they extend the spectrum of microbial secondary metabolites which comprises an enormous variety of structures. They also contribute considerably to a better understanding of the mechanism of action of a-glucosidases. These inhibitors belong to different classes of substances. Those studied most thoroughly are microbial a-glucosidase inhibitors which are members of a homologous series of pseudooligosaccharides of the general formula (4). They all have a core in common which is essential for their inhibitory action, a pseudodisaccharide residue consisting of an unsaturated cyclitol unit, and a 4-amino-4,6-dideoxyglucose unit. The-in many respects-most interesting representative of this homologous series is acarbose (5). a pseudotetrasaccharide exhibiting a very pronounced inhibitory effect on intestinal a-glucosidases such as sucrase, maltase and glucoamylase. The present paper will review this new field of microbial a-glucosidase inhibitors which has been studied with particular intensity during the past ten years. 0 Verlag Chemie GmbH. 6940 Weinheim, 1981 0570-0833/81/0909-0744 $02.50/0 Angew. Chem. lnt. Ed. Engl. 20, 744-761 (1981) [*] K , for I-deoxynojirimycin (36): 4 . 8~ from porcine small intestine, method: "Dixon plot"). mol/L at pH 6.25 (isomaltase Angew. Chem. In(. Ed. Engl. 20. 744-761 (1981)

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