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  • Title: Inactivation of alpha-glucosidase by the active-site-directed inhibitor, conduritol B epoxide.
    Author: Yang SJ, Ge SG, Zeng YC, Zhang SZ.
    Journal: Biochim Biophys Acta; 1985 Apr 29; 828(3):236-40. PubMed ID: 3886011.
    Abstract:
    Conduritol B epoxide is an active-site-directed inhibitor of some glucosidases. The inactivation of alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) from Monascus ruber by conduritol B epoxide is irreversible and first-order with respect to time and inhibitor concentration. The inactivation is prevented by the presence of the substrate maltose. The pH-dependence of Vmax for maltose indicated the participation of two dissociating groups with pK values of 4.1 and 5.8 in the enzyme-substrate complex. Modification of the alpha-glucosidase with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride led to loss of activity, which suggests that a carboxyl group(s) is located at the active site of alpha-glucosidase.
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