CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.20 | Alpha-Beta Barrel |
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3.20.20 | TIM Barrel |
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3.20.20.80 | Glycosidases |
Domain Context
CATH Clusters
Superfamily | Glycosidases |
Functional Family | Oligo-1,6-glucosidase IMA1 |
Enzyme Information
3.2.1.10 |
Oligo-1,6-glucosidase.
based on mapping to UniProt P53051
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
-!- This enzyme, like EC 3.2.1.33, can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41, EC 3.2.1.142 and EC 3.2.1.68 is maltose. -!- It also hydrolyzes 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 catalyzes the reaction of EC 3.2.1.48. -!- Differs from EC 3.2.1.33 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.
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UniProtKB Entries (1)
P53051 |
MALX3_YEAST
Saccharomyces cerevisiae S288C
Oligo-1,6-glucosidase IMA1
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PDB Structure
PDB | 3AXH |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Steric hindrance by 2 amino acid residues determines the substrate specificity of isomaltase from Saccharomyces cerevisiae
J.Biosci.Bioeng.
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