EC - Glucan 1,4-α-glucosidase

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IntEnz Enzyme Nomenclature


Accepted name:
glucan 1,4-α-glucosidase
Other names:
γ-1,4-glucan glucohydrolase
acid maltase
glucose amylase
lysosomal α-glucosidase
1,4-α-D-glucan glucohydrolase
Systematic name:
4-α-D-glucan glucohydrolase



Most forms of the enzyme can rapidly hydrolyse 1,6-α-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-α-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC α-glucosidase, from mammalian intestine, can catalyse similar reactions.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00120 , PROSITE:PDOC00646 , PROSITE:PDOC51166
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004339
CAS Registry Number: 9032-08-0
UniProtKB/Swiss-Prot: (28) [show] [UniProt]


  1. French, D. and Knapp, D.W.
    The maltase of Clostridium acetobutylicum; its specificity range and mode of action.
    J. Biol. Chem. 187 : 463-471 (1950). [PMID: 14803428]
  2. Illingworth Brown, B. and Brown, D.H.
    The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues.
    Biochim. Biophys. Acta 110 : 124-133 (1965). [PMID: 4286143]
  3. Jeffrey, P.L., Brown, D.H. and Brown, B.I.
    Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme.
    Biochemistry 9 : 1403-1415 (1970). [PMID: 4313883]
  4. Kelly, J.J. and Alpers, D.H.
    Properties of human intestinal glucoamylase.
    Biochim. Biophys. Acta 315 : 113-122 (1973). [PMID: 4743896]
  5. Miller, K.D. and Copeland, W.H.
    A blood trans-α-glucosylase.
    Biochim. Biophys. Acta 22 : 193-194 (1956). [PMID: 13373867]
  6. Tsujisaka, Y., Fukimoto, J. and Yamamoto, T.
    Specificity of crystalline saccharogenic amylase of moulds.
    Nature 181 : 770-771 (1958).

[EC created 1961]