| 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; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase; 4-α-D-glucan glucohydrolase |
| Systematic name: |
4-α-D-glucan exo β-(1→4)-glucohydrolase (non-reducing end, configuration-inverting) |
| Comments: |
Most forms of the enzyme can also 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 both (1→6)- and (1→3)-α-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes with configuration-inverting activity that act on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 α-glucosidase, from mammalian intestine, can catalyse similar reactions but prefers oligosaccharides and retains the anomeric configuration of the release glucosyl units. |
| 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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