EC 3.2.1.48 - Sucrose α-glucosidase

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IntEnz Enzyme Nomenclature
EC 3.2.1.48

Names

Accepted name:
sucrose α-glucosidase
Other names:
intestinal sucrase
sucrase
sucrase(invertase)
sucrase-isomaltase
sucrose α-glucohydrolase
sucrose.alpha.-glucohydrolase
Systematic name:
sucrose-α-D-glucohydrolase

Reaction

Comments:

This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00120
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004575
CAS Registry Number: 37288-39-4
UniProtKB/Swiss-Prot:

References

  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: 5735-5741 (1975). [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: 5183-5186 (1979). [PMID: 291933]
  3. Kolinska, J. and Kraml, J.
    Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine.
    Biochim. Biophys. Acta 284: 235-247 (1972). [PMID: 5073761]
  4. Sigrist, H., Ronner, P. and Semenza, G.
    A hydrophobic form of the small-intestinal sucrase-isomaltase complex.
    Biochim. Biophys. Acta 406: 433-446 (1975). [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: 11332-11338 (1980). [PMID: 7002920]
  6. Takesue, Y.
    Purification and properties of rabbit intestinal sucrase.
    J. Biochem. (Tokyo) 65: 545-552 (1969). [PMID: 5804876]

[EC 3.2.1.48 created 1972]