Jump to content

Glucan 1,4-α-glucosidase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Dcirovic (talk | contribs) at 23:11, 30 March 2016 (added a link to List of enzymes). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Glucan 1,4-alpha-glucosidase
Identifiers
EC no.3.2.1.3
CAS no.9032-08-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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

References

  1. ^ French, D. and Knapp, D.W. (1950). "The maltase of Clostridium acetobutylicum". J. Biol. Chem. 187: 463–471. PMID 14803428.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Illingworth Brown, B. and 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. doi:10.1016/s0926-6593(65)80101-1. PMID 4286143.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Jeffrey, P.L., Brown, D.H. and Brown, B.I. (1970). "Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry. 9: 1403–1415. doi:10.1021/bi00808a015. PMID 4313883.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Kelly, J.J. and Alpers, D.H. (1973). "Properties of human intestinal glucoamylase". Biochim. Biophys. Acta. 315: 113–122. doi:10.1016/0005-2744(73)90135-6. PMID 4743896.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ Miller, K.D. and Copeland, W.H. (1956). "A blood trans-α-glucosylase". Biochim. Biophys. Acta. 22: 193–194. doi:10.1016/0006-3002(56)90242-6. PMID 13373867.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  6. ^ Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. (1958). "Specificity of crystalline saccharogenic amylase of moulds". Nature. 181: 770–771. doi:10.1038/181770a0. PMID 13517301.{{cite journal}}: CS1 maint: multiple names: authors list (link)