EC - Oligo-1,6-glucosidase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature


Accepted name:
Other names:
α-limit dextrinase
dextrin 6-glucanohydrolase
dextrin 6α-glucanohydrolase
limit dextrinase (erroneous)
oligosaccharide α-1,6-glucosidase
Systematic name:
oligosaccharide α-1,6-glucohydrolase



This enzyme, like EC (amylo-α-1,6-glucosidase), can release an α-1→6-linked glucose, whereas the shortest chain that can be released by EC (pullulanase), EC (limit dextrinase), and EC (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC (sucrose α-glucosidase). Differs from EC (amylo-α-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00120
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004574
CAS Registry Number: 9032-15-9
UniProtKB/Swiss-Prot: (18) [show] [UniProt]


  1. 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]
  2. 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]
  3. Rodriguez, I.R., Taravel, F.R. and Whelan, W.J.
    Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits.
    Eur J Biochem. 143 : 575-582 (1984). [PMID: 6479163]
  4. Khan, N. A., Eaton, N. R.
    Purification and characterization of maltase and alpha-methyl glucosidase from yeast.
    Biochim. Biophys. Acta 146 : 173-180 (1967). [PMID: 6060462]
  5. Yamamoto, K., Nakayama, A., Yamamoto, Y., Tabata, S.
    Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae.
    Eur. J. Biochem. 271 : 3414-3420 (2004). [PMID: 15291818]

[EC created 1961, modified 2000]