The Enzyme Database

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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, 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. [PMID: 4743896]
5.  Miller, K.D. and Copeland, W.H. A blood trans-α-glucosylase. Biochim. Biophys. Acta 22 (1956) 193–194. [PMID: 13373867]
6.  Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. Specificity of crystalline saccharogenic amylase of moulds. Nature 181 (1958) 770–771. [PMID: 13517301]
[EC 3.2.1.3 created 1961]
 
 


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