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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.
Alglucosidase alfa is indicated for people with Pompe disease (GAA deficiency). [1]In 2014 the U.S. Food and Drug Administration announced the approval of alglucosidase alfa for treatment of people with infantile-onset Pompe disease, including people who are less than eight years of age.
Beta-glucosidase # EC 3.2.1.21 : is associated with Gaucher's disease: Lactase: EC 3.2.1.23 : one member of the β-galactosidase family, breaks down milk sugars, and its absence in adulthood causes lactose intolerance: Debranching enzyme # EC 3.2.1.33: in mammals, yeast and some bacteria, combines transferase and glucosidase activity in ...
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] In humans, it is encoded by the GAA gene. [5]
Glucan 1,3-α-glucosidase (EC 3.2.1.84, exo-1,3-α-glucanase, glucosidase II, 1,3-α-D-glucan 3-glucohydrolase) is an enzyme with systematic name 3-α-D-glucan 3-glucohydrolase. [1] It catalyses the hydrolysis of terminal (1→3)-α-D-glucosidic links in (1→3)-α-D-glucans. It does not act on nigeran although it has some activity against ...
The most significant oligosaccharide β-glucosidase reacts with is cellulose. Cellulose is a polymer composed of β-1,4-linked glucosyl residues. β-glucosidases, cellulases (endoglucanases), cellobiosidases (exoglucanases) are required by a number of organisms to consume it. These enzymes are powerful tools for degradation of plant cell walls ...
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 ...
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]