[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/sucrose-alpha-glucosidase-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/sucrose-alpha-glucosidase-wikipedia\/","headline":"Sucrose alpha-glucosidase – Wikipedia","name":"Sucrose alpha-glucosidase – Wikipedia","description":"From Wikipedia, the free encyclopedia Sucrose alpha-glucosidase (EC 3.2.1.48, sucrose alpha-glucohydrolase, sucrase, sucrase-isomaltase, sucrose.alpha.-glucohydrolase, intestinal sucrase, sucrase(invertase)) is an enzyme","datePublished":"2014-06-15","dateModified":"2014-06-15","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/www.wikimedia.org\/static\/images\/wmf-logo.png","url":"https:\/\/www.wikimedia.org\/static\/images\/wmf-logo.png","height":"101","width":"135"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/sucrose-alpha-glucosidase-wikipedia\/","about":["Wiki"],"wordCount":2973,"articleBody":"From Wikipedia, the free encyclopediaSucrose alpha-glucosidase (EC 3.2.1.48, sucrose alpha-glucohydrolase, sucrase, sucrase-isomaltase, sucrose.alpha.-glucohydrolase, intestinal sucrase, sucrase(invertase)) is an enzyme with systematic name sucrose-alpha-D-glucohydrolase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reactionHydrolysis of sucrose and maltose by an alpha-D-glucosidase-type actionThis enzyme is isolated from intestinal mucosa as a single polypeptide chain. The human sucrase-isomaltase is a dual-function enzyme with two GH31 domains, one serving as the isomaltase, the other serving as a sucrose alpha-glucosidase.References[edit]^ Conklin KA, Yamashiro KM, Gray GM (August 1975). “Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits”. The Journal of Biological Chemistry. 250 (15): 5735\u201341. doi:10.1016\/S0021-9258(19)41116-2. PMID\u00a0807575.^ Hauri HP, Quaroni A, Isselbacher KJ (October 1979). “Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase”. Proceedings of the National Academy of Sciences of the United States of America. 76 (10): 5183\u20136. doi:10.1073\/pnas.76.10.5183. PMC\u00a0413104. PMID\u00a0291933.^ Kol\u00ednsk\u00e1 J, Kraml J (September 1972). “Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine”. Biochimica et Biophysica Acta (BBA) – Enzymology. 284 (1): 235\u201347. doi:10.1016\/0005-2744(72)90062-9. PMID\u00a05073761.^ Sigrist H, Ronner P, Semenza G (October 1975). “A hydrophobic form of the small-intestinal sucrase-isomaltase complex”. Biochimica et Biophysica Acta (BBA) – Biomembranes. 406 (3): 433\u201346. doi:10.1016\/0005-2736(75)90022-x. PMID\u00a01182172.^ Sj\u00f6str\u00f6m H, Nor\u00e9n O, Christiansen L, Wacker H, Semenza G (December 1980). “A fully active, two-active-site, single-chain sucrase.isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein”. The Journal of Biological Chemistry. 255 (23): 11332\u20138. doi:10.1016\/S0021-9258(19)70296-8. PMID\u00a07002920.^ Takesue Y (April 1969). “Purification and properties of rabbit intestinal sucrase”. Journal of Biochemistry. 65 (4): 545\u201352. doi:10.1093\/oxfordjournals.jbchem.a129048. 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