Biology:Glucan 1,4-a-glucosidase
| Glucan 1,4-α-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glucoamylase homohexamer, Penicillium oxalicum | |||||||||
| 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-α-glucosidase (EC 3.2.1.3, glucoamylase, amyloglucosidase', γ-amylase, lysosomal α-glucosidase, acid maltase, exo-1,4-α-glucosidase, glucose amylase, γ-1,4-glucan glucohydrolase, acid maltase, 1,4-α-D-glucan glucohydrolase) is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase.[1][2][3][4][5][6] It catalyses the following chemical reaction
- Hydrolysis of terminal (1→4)-linked α-D-glucose residues successively from non-reducing ends of the chains with release of β-D-glucose
Most forms of the enzyme can rapidly hydrolyse 1,6-α-D-glucosidic bonds when the next bond in the sequence is 1,4. They belong to a variety of different GH families, such as glycoside hydrolase family 15 in fungi, glycoside hydrolase family 31 of human intestine MGAM, and glycoside hydrolase family 97 of bacterial forms. It was also known as γ-Amylase.
See also
References
- ↑ "The maltase of Clostridium acetobutylicum; its specificity range and mode of action". The Journal of Biological Chemistry 187 (2): 463–71. December 1950. doi:10.1016/S0021-9258(18)56190-1. PMID 14803428.
- ↑ "The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues". Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation 110 (1): 124–33. October 1965. doi:10.1016/s0926-6593(65)80101-1. PMID 4286143.
- ↑ "Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry 9 (6): 1403–15. March 1970. doi:10.1021/bi00808a015. PMID 4313883.
- ↑ "Properties of human intestinal glucoamylase". Biochimica et Biophysica Acta (BBA) - Enzymology 315 (1): 113–22. July 1973. doi:10.1016/0005-2744(73)90135-6. PMID 4743896.
- ↑ "A blood trans-α-glucosylase". Biochimica et Biophysica Acta 22 (1): 193–4. October 1956. doi:10.1016/0006-3002(56)90242-6. PMID 13373867.
- ↑ "Specificity of crystalline saccharogenic amylase of moulds". Nature 181 (4611): 770–1. March 1958. doi:10.1038/181770a0. PMID 13517301. Bibcode: 1958Natur.181..770T.
External links
- Glucan+1,4-alpha-glucosidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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