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- W2013998503 abstract "Methods are described for the preparation and subsequent 18O determination of [I-18O]maltose. Starch was hydrolysed in H218O by α- and β-amylases and the maltose and glucose produced were analysed for their 18O content. It is shown that all the 18O is bound to the anomeric carbon atoms of the sugar molecules, proving that the enzyme splits the bond C1OC4 at C1. This accords with the assumption that β-amylase catalyzes bond fission by a single displacement mechanism, while α-amylase catalyzes the same bond cleavage by a double displacement mechanism with subsequent retention of the configuration. It is concluded that glucosidic bond cleavage is not always accompanied by a Walden inversion. The inversion is affected by the exact orientation of the active and complementary groups of the enzyme and substrate." @default.
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- W2013998503 modified "2023-10-07" @default.
- W2013998503 title "On the mechanism of the glucosidic bond cleavage in the enzymic hydrolysis of starch" @default.
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- W2013998503 doi "https://doi.org/10.1016/0006-3002(59)90065-4" @default.
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