Glucan 1,4-a-glucosidase

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Glucan 1,4-alpha-glucosidase
EC number3.2.1.3
CAS number9032-08-0
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Glucan 1,4-alpha-glucosidase (EC, glucoamylase, amyloglucosidase (AMG), 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]


  1. ^ French D, Knapp DW (December 1950). "The maltase of Clostridium acetobutylicum; its specificity range and mode of action". The Journal of Biological Chemistry. 187 (2): 463–71. PMID 14803428.
  2. ^ Brown BI, Brown DH (October 1965). "The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-alpha-1,4-glucan glucohydrolase in human tissues". Biochimica et Biophysica Acta. 110 (1): 124–33. doi:10.1016/s0926-6593(65)80101-1. PMID 4286143.
  3. ^ Jeffrey PL, Brown DH, Brown BI (March 1970). "Studies of lysosomal alpha-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry. 9 (6): 1403–15. doi:10.1021/bi00808a015. PMID 4313883.
  4. ^ Kelly JJ, Alpers DH (July 1973). "Properties of human intestinal glucoamylase". Biochimica et Biophysica Acta. 315 (1): 113–22. doi:10.1016/0005-2744(73)90135-6. PMID 4743896.
  5. ^ Copeland WH, Miller KD (October 1956). "A blood trans-alpha-glucosylase". Biochimica et Biophysica Acta. 22 (1): 193–4. doi:10.1016/0006-3002(56)90242-6. PMID 13373867.
  6. ^ Tsujisaka Y, Fukumoto J, Yamamcto T (March 1958). "Specificity of crystalline saccharogenic amylase of moulds". Nature. 181 (4611): 770–1. doi:10.1038/181770a0. PMID 13517301.

External links[edit]