The Enzyme Database

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Accepted name: sucrose α-glucosidase
Reaction: Hydrolysis of sucrose and maltose by an α-D-glucosidase-type action
Other name(s): sucrose α-glucohydrolase; sucrase; sucrase-isomaltase; sucrose.α.-glucohydrolase; intestinal sucrase; sucrase(invertase)
Systematic name: sucrose-α-D-glucohydrolase
Comments: This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC oligo-1,6-glucosidase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37288-39-4
1.  Conklin, K.A., Yamashiro, K.M. and Gray, G.M. Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits. J. Biol. Chem. 250 (1975) 5735–5741. [PMID: 807575]
2.  Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA 76 (1979) 5183–5186. [DOI] [PMID: 291933]
3.  Kolinska, J. and Kraml, J. Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine. Biochim. Biophys. Acta 284 (1972) 235–247. [DOI] [PMID: 5073761]
4.  Sigrist, H., Ronner, P. and Semenza, G. A hydrophobic form of the small-intestinal sucrase-isomaltase complex. Biochim. Biophys. Acta 406 (1975) 433–446. [DOI] [PMID: 1182172]
5.  Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. 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. J. Biol. Chem. 255 (1980) 11332–11338. [PMID: 7002920]
6.  Takesue, Y. Purification and properties of rabbit intestinal sucrase. J. Biochem. (Tokyo) 65 (1969) 545–552. [PMID: 5804876]
[EC created 1972]

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