Search results
Results from the WOW.Com Content Network
Alpha-glucosidase inhibitors (AGIs) are oral anti-diabetic drugs used for diabetes mellitus type 2 that work by preventing the digestion of carbohydrates (such as starch and table sugar). They are found in raw plants/herbs such as cinnamon and bacteria (containing the inhibitor acarbose ).
It is defined as "catalysis of the hydrolysis of terminal, non-reducing alpha-linked alpha-D-glucose residue with release of alpha-D-glucose." In this sense, "alpha-glucosidase" can encompass a wide range of enzyme activitiess, differing by the linkage of their terminal (1→3, 1→4, or 1→6), the specific identity of their substrate (sucrose ...
Alpha-glucosidases are enzymes involved in breaking down complex carbohydrates such as starch and glycogen into their monomers. [2] They catalyze the cleavage of individual glucosyl residues from various glycoconjugates including alpha- or beta-linked polymers of glucose. This enzyme convert complex sugars into simpler ones.
From these natural templates many other inhibitors have been developed, including isofagomine and deoxygalactonojirimycin, and various unsaturated compounds such as PUGNAc. Inhibitors that are in clinical use include the anti-diabetic drugs acarbose and miglitol, and the antiviral drugs oseltamivir and zanamivir. Some proteins have been found ...
Aspergillusol A is an alpha-glucosidase inhibitor isolated from marine Aspergillus. [2] Structurally, it consists of an erythritol group in the center, with two hydroxyimino-phenylpropanoyl groups attached to it from either side.
Alpha-glucosidase inhibitors are a class of diabetes drugs found in plants/herbs like cinnamon; [3] however, they are technically not hypoglycemic agents because they do not have a direct effect on insulin secretion or sensitivity. These agents slow the digestion of starch in the small intestine, such that glucose from the starch enters the ...
Maltase-glucoamylase is an alpha-glucosidase digestive enzyme. It consists of two subunits with differing substrate specificity. Recombinant enzyme studies have shown that its N-terminal catalytic domain has highest activity against maltose, while the C-terminal domain has a broader substrate specificity and activity against glucose oligomers. [7]
Pages in category "Alpha-glucosidase inhibitors" The following 6 pages are in this category, out of 6 total. This list may not reflect recent changes. A. Acarbose;