CATH Classification

Domain Context

CATH Clusters

Superfamily Spasmolytic Protein, domain 1
Functional Family Maltase-glucoamylase, intestinal

Enzyme Information

3.2.1.20
Alpha-glucosidase.
based on mapping to UniProt O43451
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
-!- Group of enzymes whose specificity is directed mainly toward the exohydrolysis of 1,4-alpha-glucosidic linkages, and that hydrolyze oligosaccharides rapidly, relative to polysaccharides, which are hydrolyzed relatively slowly, or not at all. -!- The intestinal enzyme also hydrolyzes polysaccharides, catalyzing the reactions of EC 3.2.1.3, and, more slowly, hydrolyzes 1,6-alpha-D- glucose links.
3.2.1.3
Glucan 1,4-alpha-glucosidase.
based on mapping to UniProt O43451
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D- glucose.
-!- Most forms of the enzyme can rapidly hydrolyze 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyze 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. -!- This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. -!- EC 3.2.1.20 from mammalian intestine can catalyze similar reactions.

UniProtKB Entries (1)

O43451
MGA_HUMAN
Homo sapiens
Maltase-glucoamylase, intestinal

PDB Structure

PDB 3TON
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural insight into substrate specificity of human intestinal maltase-glucoamylase
Ren, L.M., Qin, X.H., Cao, X.F., Wang, L.L., Bai, F., Bai, G., Shen, Y.
Protein Cell