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.
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.
6. Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. Specificity of crystalline saccharogenic amylase of moulds. Nature 181 (1958) 770-771.