Glucan 1,4-a-glucosidase

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Glucan 1,4-alpha-glucosidase
Identifiers
EC number 3.2.1.3
CAS number 9032-08-0
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Glucan 1,4-alpha-glucosidase (EC 3.2.1.3, glucoamylase, amyloglucosidase, gamma-amylase, lysosomal alpha-glucosidase, acid maltase, exo-1,4-alpha-glucosidase, glucose amylase, gamma-1,4-glucan glucohydrolase, acid maltase, 1,4-alpha-D-glucan glucohydrolase) is an enzyme located on the brush border of the small intestine with systematic name 4-alpha-D-glucan glucohydrolase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction

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 hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4.

See also[edit]

References[edit]

  1. ^ French, D.; Knapp, D.W. (1950). "The maltase of Clostridium acetobutylicum". J. Biol. Chem. 187: 463–471. PMID 14803428. 
  2. ^ Illingworth Brown, B.; Brown, D.H. (1965). "The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues". Biochim. Biophys. Acta. 110: 124–133. PMID 4286143. doi:10.1016/s0926-6593(65)80101-1. 
  3. ^ Jeffrey, P.L.; Brown, D.H.; Brown, B.I. (1970). "Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry. 9: 1403–1415. PMID 4313883. doi:10.1021/bi00808a015. 
  4. ^ Kelly, J.J.; Alpers, D.H. (1973). "Properties of human intestinal glucoamylase". Biochim. Biophys. Acta. 315: 113–122. PMID 4743896. doi:10.1016/0005-2744(73)90135-6. 
  5. ^ Miller, K.D.; Copeland, W.H. (1956). "A blood trans-α-glucosylase". Biochim. Biophys. Acta. 22: 193–194. PMID 13373867. doi:10.1016/0006-3002(56)90242-6. 
  6. ^ Tsujisaka, Y.; Fukimoto, J.; Yamamoto, T. (1958). "Specificity of crystalline saccharogenic amylase of moulds". Nature. 181: 770–771. PMID 13517301. doi:10.1038/181770a0. 

External links[edit]