EC 3 - Hydrolases
EC 3.2 - Glycosylases
EC 3.2.1 - Glycosidases, i.e. enzymes hydrolyzing O- and S-glycosyl compounds
EC 3.2.1.10 - Oligo-1,6-glucosidase
IntEnz Enzyme Nomenclature
EC 3.2.1.10
Names
dextrin 6-glucanohydrolase
dextrin 6α-glucanohydrolase
exo-oligo-1,6-glucosidase
isomaltase
limit dextrinase (erroneous)
sucrase-isomaltase
oligosaccharide α-1,6-glucosidase
α-methylglucosidase
Reaction
- Hydrolysis of (1right6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Comments:
This enzyme, like EC 3.2.1.33 (amylo-α-1,6-glucosidase), can release an α-1→6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose α-glucosidase). Differs from EC 3.2.1.33 (amylo-α-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
Links to other databases
References
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Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase.Proc. Natl. Acad. Sci. USA 76 : 5183-5186 (1979). [PMID: 291933]
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A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein.J. Biol. Chem. 255 : 11332-11338 (1980). [PMID: 7002920]
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Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits.Eur J Biochem. 143 : 575-582 (1984). [PMID: 6479163]
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Purification and characterization of maltase and alpha-methyl glucosidase from yeast.Biochim. Biophys. Acta 146 : 173-180 (1967). [PMID: 6060462]
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Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae.Eur. J. Biochem. 271 : 3414-3420 (2004). [PMID: 15291818]
[EC 3.2.1.10 created 1961, modified 2000]