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: 4-α-D-glucoside exo α-(1,4)-glucohydrolase (non-reducing end, configuration-retaining)
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 a reaction similar to EC 3.2.1.3, glucan 1,4-α-glucosidase, but releasing α- rather than β-glucose residues. The enzyme can also hydrolyse 1,6-α-D-glucose links, but more slowly.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9001-42-7
References:
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]