[Comparative study of glycosidase from cattle liver and exoglycanase from Aspergillus awamori].
Anomerities of products were estimated for glucosidases from cattle liver and Aspergillus awamori. It was demonstrated that the enzyme from cattle liver is alpha-glucosidase and that from Asp. awamori is exogluconase. It was demonstrated that alpha-glucosidase hydrolyzes the C1--O bond in the course of reaction. delta-Lactone of gluconic acid is a competitive inhibitor for both enzymes. The secondary kinetic isotope effects for both enzymes were measured. The isotope effect for alpha-glucosidase is equal to 1, for exogluconase 1,1 for glycogen and 1,18 for maltose. Some aspects of mechanisms of both enzymes are discussed in terms of the data obtained.
D000818:Animals; D001230:Aspergillus / Q000201:enzymology*; D001665:Binding Sites; D002417:Cattle; D005959:Glucosidases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D013379:Substrate Specificity; D000520:alpha-Glucosidases / Q000378:metabolism
D005959:Glucosidases; D006026:Glycoside Hydrolases; D000520:alpha-Glucosidases
Sravnitel'noe izuchenie mekhanizma deĭstviia gliukozidazy iz pecheni byka i ekzogliukonazy iz Aspergillus awamori.