EC 188.8.131.52 - Glucan 1,4-α-glucosidase
IntEnz Enzyme Nomenclature
- Hydrolysis of terminal (1→4)-linked α-D-glucose residues successively from non-reducing ends of the chains with release of β-D-glucose
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 184.108.40.206 α-glucosidase, from mammalian intestine, can catalyse similar reactions.
Links to other databases
The maltase of Clostridium acetobutylicum; its specificity range and mode of action.J. Biol. Chem. 187: 463-471 (1950). [PMID: 14803428]
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]
Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme.Biochemistry 9: 1403-1415 (1970). [PMID: 4313883]
Properties of human intestinal glucoamylase.Biochim. Biophys. Acta 315: 113-122 (1973). [PMID: 4743896]
A blood trans-α-glucosylase.Biochim. Biophys. Acta 22: 193-194 (1956). [PMID: 13373867]
Specificity of crystalline saccharogenic amylase of moulds.Nature 181: 770-771 (1958).
[EC 220.127.116.11 created 1961]