IUBMB Enzyme Nomenclature


Accepted name: α-glucosidase

Reaction: Hydrolysis of terminal, non-reducing (1→4)-linked α-D-glucose residues with release of α-D-glucose

Other name(s): maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinvertase; α-D-glucosidase; α-glucoside hydrolase; α-1,4-glucosidase

Systematic name: α-D-glucoside glucohydrolase

Comments: This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of 1,4-α-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC glucan 1,4-α-glucosidase and, more slowly, hydrolyses 1,6-α-D-glucose links.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-42-7


1. Bruni, C.B., Sica, V., Auricchio, F. and Covelli, I. Further kinetic and structural characterization of the lysosomal α-D-glucoside glucohydrolase from cattle liver. Biochim. Biophys. Acta 212 (1970) 470-477. [PMID: 5466143]

2. Flanagan, P.R. and Forstner, G.G. Purification of rat intestinal maltase/glucoamylase and its anomalous dissociation either by heat or by low pH. Biochem. J. 173 (1978) 553-563. [PMID: 29602]

3. Larner, J. Other glucosidases, in Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York , 1960, pp. 369-378.

4. Sivikami, S. and Radhakrishnan, A.N. Purification of rabbit intestinal glucoamylase by affinity chromatography on Sephadex G-200. Indian J. Biochem. Biophys. 10 (1973) 283-284. [PMID: 4792946]

5. Sørensen, S.H., Norén, O., Sjöström, H. and Danielsen, E.M. Amphiphilic pig intestinal microvillus maltase/glucoamylase. Structure and specificity. Eur. J. Biochem. 126 (1982) 559-568. [PMID: 6814909]

[EC created 1961]

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