ENZYME entry: EC 3.2.1.3

Accepted Name
Glucan 1,4-alpha-glucosidase.
Alternative Name(s)
4-alpha-D-glucan glucohydrolase.
Amyloglucosidase.
Exo-1,4-alpha-glucosidase.
Gamma-amylase.
Glucoamylase.
Lysosomal alpha-glucosidase.
Reaction catalysed
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
Comment(s)
  • 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.
Cross-references
PROSITEPDOC00120 ; PDOC00646 ; PDOC51166
BRENDA3.2.1.3
EC2PDB3.2.1.3
ExplorEnz3.2.1.3
PRIAM enzyme-specific profiles3.2.1.3
KEGG Ligand Database for Enzyme Nomenclature3.2.1.3
IUBMB Enzyme Nomenclature3.2.1.3
IntEnz3.2.1.3
MEDLINEFind literature relating to 3.2.1.3
MetaCyc3.2.1.3
UniProtKB/Swiss-Prot
P69327, AMYG_ASPAW;  P23176, AMYG_ASPKA;  P69328, AMYG_ASPNG;  
P36914, AMYG_ASPOR;  P22832, AMYG_ASPSH;  P42042, AMYG_BLAAD;  
O74254, AMYG_CANAL;  P29761, AMYG_CLOS0;  Q03045, AMYG_HORRE;  
P14804, AMYG_NEUCR;  P07683, AMYG_RHIOR;  P08017, AMYG_SACFI;  
P22861, AMYG_SCHOC;  O60087, AMYG_SCHPO;  P08019, AMYG_YEAST;  
P26989, AMYH_SACFI;  P04065, AMYH_YEASX;  P29760, AMYI_YEASX;  
O43451, MGA_HUMAN;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.2.-.-
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