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α-Glucosidase hydrolyzes terminal non-reducing (1→4)-linked α-glucose residues to release a single α-glucose molecule. [ 10 ] α-Glucosidase is a carbohydrate-hydrolase that releases α-glucose as opposed to β-glucose. β-Glucose residues can be released by glucoamylase, a functionally similar enzyme.
EC 3.2.1.3 : is a digestive enzyme Cellulase # EC 3.2.1.4 : breaks down cellulose from plant material Sucrase-isomaltase: EC 3.2.1.10 - Mannosyl-oligosaccharide glucosidase # EC 3.2.1.106 catalyzes the first trimming step of the N-glycosylation pathway; is associated with Congenital Disorder of Glycosylation type IIb: Acid α-glucosidase # EC 3 ...
Chemically, the drug is an analog of the enzyme that is deficient in patients affected by Pompe disease, alpha-glucosidase. It is the first drug available to treat this disease. [2] It was approved for medical use in the United States in April 2006, as Myozyme [7] and in May 2010, as Lumizyme. [8]
Amylo-α-1,6-glucosidase (EC 3.2.1.33), or glucosidase, cleaves the remaining alpha-1,6 linkage, producing glucose and a linear chain of glycogen. [10] The mechanism by which the glucosidase cleaves the α -1,6-linkage is not fully known because the amino acids in the active site have not yet been identified.
Acid alpha-glucosidase, also called acid maltase, [5] is an enzyme that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme , but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol. [ 6 ]
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 ).
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]
[4] [5] Cipaglucosidase alfa is a recombinant human acid α-glucosidase enzyme replacement therapy that provides an exogenous source of acid α-glucosidase. [ 5 ] The most common side effects include chills, dizziness, flushing, sleepiness, chest discomfort, cough, swelling at the infusion site and pain. [ 5 ]