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- W2017102412 abstract "Inhibitory activities of 1-deoxynojirimycin and gluconolactone on Aspergillus niger glucoamylase were studied in relation to the subsite structure of the enzyme. Although both of these inhibitors are considered to bind at subsite 1 of the enzyme active site, 1-deoxynojirimycin showed competitive type inhibition but gluconolactone was a mixed type (or noncompetitive type) inhibitor for the hydrolysis of p-nitrophenyl alpha-D-glucoside. The former type of inhibition suggested that the main binding mode of the substrate was productive, but the latter, nonproductive. A possible way of explaining these apparent inconsistent results is to assume that the main binding mode of the substrate is productive and gluconolactone forms a nonproductive ternary complex with the enzyme and the substrate." @default.
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- W2017102412 date "1999-01-01" @default.
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- W2017102412 title "Steady-State Inhibitory Kinetic Studies on the Ligand Binding Modes of<i>Aspergillus niger</i>Glucoamylase" @default.
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- W2017102412 doi "https://doi.org/10.1271/bbb.63.1548" @default.
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