Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The inhibitory action and mechanism of inhibition of two types of alpha-glucosidase inhibitors, acarbose (Bay-g-5421) and 1-deoxynojirimycin derivatives (Bay-m-1099 and Bay-o-1248), on small intestinal carbohydrases (sucrase, isomaltase, glucoamylase, trehalase and lactase) and pancreatic alpha-amylase were compared in vitro using small intestinal brush border membranes and pancreatic homogenates from adult Sprague-Dawley rats. Acarbose at a low (4 microM) concentration strongly inhibited the activities of glucoamylase, alpha-amylase and sucrase (98, 68, and 63%, respectively). At a high (200 microM) concentration, isomaltase activity was also inhibited (28%); effects on trehalase and lactase activities were negligible. Both the 1-deoxynojirimycin derivatives were even more potent inhibitors of sucrase (Ki = 8.6 x 10(-8) M for Bay-m-1099;Ki = 5.0 X 10(-8) M for Bay-o-1248) than acarbose (Ki = 9.9 x 10(-7) M). Whereas glucoamylase activity was strongly inhibited by the 1-deoxynojirimycin derivatives, alpha-amylase activity was not. In contrast to acarbose, the 1-deoxynojirimycin derivatives at high concentrations (20-200 microM) inhibited considerably trehalase and lactase (a beta-galactosidase) activities. The inhibition of lactase activity was stronger by Bay-m-1099 (Ki = 4.9 X 10(-6) M) than by Bay-o-1248 (Ki = 6.7 X 10(-5) M). Where inhibition was seen, kinetic analysis showed fully competitive inhibition of sucrase, isomaltase, trehalase, glucoamylase and lactase by all three inhibitors.
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PMID:Inhibitory mechanism of acarbose and 1-deoxynojirimycin derivatives on carbohydrases in rat small intestine. 296 44

Acarbose analogues, containing cellobiose and lactose structures, were prepared by reaction of the two disaccharides with acarbose and Bacillus stearothermophilus maltogenic amylase. The kinetics for the inhibition by the two analogues was studied for beta-glucosidase, beta-galactosidase, cyclomaltodextrin glucanosyltransferase (CGTase), and alpha-glucosidase. Both analogues were potent competitive inhibitors for beta-glucosidase, with K(I) values in the range of 0.04-2.44 microM, and the lactose analogues were good uncompetitive inhibitors for beta-galactosidase, with K(I) values in the range of 159-415 microM, while acarbose was not an inhibitor for either enzyme at 10 and 5 mM, respectively. Both analogues were also potent mixed inhibitors for CGTase, with K(I) values in the range of 0.1-9.3 microM. The lactose analogue was a 6.4-fold better competitive inhibitor for alpha-glucosidase than was acarbose.
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PMID:Inhibition of beta-glycosidases by acarbose analogues containing cellobiose and lactose structures. 1128 1