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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. The substrate selectivity of α ...
is a plant enzyme to break down starch: γ-Amylase: 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 ...
Glycogen debranching enzyme then transfers three of the remaining four glucose units to the end of another glycogen branch. This exposes the α[1→6] branching point, which is hydrolysed by α[1→6] glucosidase, removing the final glucose residue of the branch as a molecule of glucose and eliminating the branch. This is the only case in which ...
Mechanism for cleaving of alpha-1,6 linkage. 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 ...
Glycoside hydrolases are classified into EC 3.2.1 as enzymes catalyzing the hydrolysis of O- or S-glycosides. Glycoside hydrolases can also be classified according to the stereochemical outcome of the hydrolysis reaction: thus they can be classified as either retaining or inverting enzymes. [6]
Glucose-6-phosphate can then progress through glycolysis. [1] Glycolysis only requires the input of one molecule of ATP when the glucose originates in glycogen. [1] Alternatively, glucose-6-phosphate can be converted back into glucose in the liver and the kidneys, allowing it to raise blood glucose levels if necessary. [2]
Since alpha-glucosidase inhibitors prevent the degradation of complex carbohydrates into glucose, the carbohydrates will remain in the intestine. In the colon, bacteria will digest the complex carbohydrates, thereby causing gastrointestinal side effects such as flatulence and diarrhea. Since these effects are dose-related, it is generally ...
The mechanism of all FamilyGH13 enzymes is to break a α-glucosidase linkage by hydrolyzing it. Maltase focuses on breaking apart maltose, a disaccharide that is a link between 2 units of glucose, at the α-(1->4) bond. The rate of hydrolysis is controlled by the size of the substrate (carbohydrate size). [6]