CATH Classification

Domain Context

CATH Clusters

Superfamily Golgi alpha-mannosidase II
Functional Family Maltase-glucoamylase, intestinal

Enzyme Information

3.2.1.10
Oligo-1,6-glucosidase.
based on mapping to UniProt P14410
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.
3.2.1.48
Sucrose alpha-glucosidase.
based on mapping to UniProt P14410
Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.
-!- Isolated from intestinal mucosa as a single polypeptide chain also displaying activity toward isomaltose (EC 3.2.1.10).

UniProtKB Entries (1)

P14410
SUIS_HUMAN
Homo sapiens
Sucrase-isomaltase, intestinal

PDB Structure

PDB 3LPO
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
Sim, L., Willemsma, C., Mohan, S., Naim, H.Y., Pinto, B.M., Rose, D.R.
J.Biol.Chem.