oligo-1,6-glucosidase;
limit dextrinase (erroneous);
isomaltase;
sucrase-isomaltase;
exo-oligo-1,6-glucosidase;
dextrin 6alpha-glucanohydrolase;
alpha-limit dextrinase;
dextrin 6-glucanohydrolase;
oligosaccharide alpha-1,6-glucohydrolase;
alpha-methylglucosidase

Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

oligosaccharide 6-alpha-glucohydrolase

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose

(other) R00801 R01718 R01791 R06080(G) R06087(G) R06199(G)

This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can release an alpha-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 alpha-glucosidase). Differs from EC 3.2.1.33 (amylo-alpha-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.

1  [PMID:291933]

Hauri HP, Quaroni A, Isselbacher KJ.

Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase.

Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 5183-6.

Rattus norvegicus [GN:rno]

2  [PMID:7002920]

Sjostrom H, Noren O, Christiansen L, Wacker H, Semenza G.

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 (1980) 11332-8.

Sus scofa [GN:ssc]

3  [PMID:6479163]

Rodriguez IR, Taravel FR, Whelan WJ.

Characterization and function of pig intestinal sucrase-isomaltase and its separate subunits.

Eur. J. Biochem. 143 (1984) 575-82.

Sus scofa [GN:ssc]

4  [PMID:6060462]

Khan NA, Eaton NR

Purification and characterization of maltase and alpha-methyl glucosidase from yeast.

Biochim. Biophys. Acta. 146 (1967) 173-80.

5  [PMID:15291818]

Yamamoto K, Nakayama A, Yamamoto Y, Tabata S

Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae.

Eur. J. Biochem. 271 (2004) 3414-20.