EC |
3.2.1.3 |
Accepted name: |
glucan 1,4-α-glucosidase |
Reaction: |
Hydrolysis of terminal (1→4)-linked α-D-glucose residues successively from non-reducing ends of the chains with release of β-D-glucose |
Other name(s): |
glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase |
Systematic name: |
4-α-D-glucan glucohydrolase |
Comments: |
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 3.2.1.20 α-glucosidase, from mammalian intestine, can catalyse similar reactions. |
Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9032-08-0 |
References: |
1. |
French, D. and Knapp, D.W. The maltase of Clostridium acetobutylicum. J. Biol. Chem. 187 (1950) 463–471. [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 (1965) 124–133. [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 (1970) 1403–1415. [PMID: 4313883] |
4. |
Kelly, J.J. and Alpers, D.H. Properties of human intestinal glucoamylase. Biochim. Biophys. Acta 315 (1973) 113–122. [DOI] [PMID: 4743896] |
5. |
Miller, K.D. and Copeland, W.H. A blood trans-α-glucosylase. Biochim. Biophys. Acta 22 (1956) 193–194. [DOI] [PMID: 13373867] |
6. |
Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. Specificity of crystalline saccharogenic amylase of moulds. Nature 181 (1958) 770–771. [PMID: 13517301] |
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[EC 3.2.1.3 created 1961] |
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