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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.
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 ...
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]
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]
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]
β-Glucuronidases are members of the glycosidase family of enzymes that catalyze breakdown of complex carbohydrates. [2] Human β-glucuronidase is a type of glucuronidase (a member of glycosidase Family 2) that catalyzes hydrolysis of β-D-glucuronic acid residues from the non-reducing end of mucopolysaccharides (also referred to as glycosaminoglycans) such as heparan sulfate.
Hydrolysis reaction of Maltose being broken at the 1-4 alpha-glucosidase linkage. 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.
69983 Ensembl ENSG00000090402 ENSMUSG00000027790 UniProt P14410 F8VQM5 RefSeq (mRNA) NM_001041 NM_001081137 RefSeq (protein) NP_001032 NP_001074606 Location (UCSC) Chr 3: 164.98 – 165.08 Mb Chr 3: 72.8 – 72.88 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Sucrase-isomaltase is a bifunctional glucosidase (sugar-digesting enzyme) located on the brush border of the small intestine ...