Evidence of Intramolecular Transglucosylation Catalyzed by an .ALPHA.-Glucosidase.

概要

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The hydrolytic reaction of carbohydrate-hydrolase is essentially accompanied by a reverse reaction (the condensation reaction), meaning that only the substrate capable of being hydrolyzed is produced by the reverse reaction. Honeybee α-glucosidase I can't hydrolyze isomaltose, but is capable of hydrolyzing maltose, kojibiose and slightly nigerose. Nevertheless, the enzyme catalyzes the formation and accumulation of isomaltose from glucose together with α-glucobioses such as maltose, kojibiose and nigerose. This finding is in conflict with the data that the enzyme has no hydrolytic activity toward isomaltose. However, the conflict for the peculiar phenomenon on the reaction was rationally explained by the evidence that isomaltose might be formed by the intramolecular transglucosylation via other α-glucobioses that are easily produced from glucose by the condensation reaction. It is suggested that the usual transglycosylation of carbohydrate-hydrolase may be accompanied by an intramolecular transfer reaction.
日本応用糖質科学会の論文