| Glucan 1,4-α-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glucoamylase homohexamer, Penicillium oxalicum | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.1.3 | ||||||||
| CAS no. | 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 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
- ^ 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. doi:10.1016/S0021-9258(18)56190-1. PMID 14803428.
- ^ Brown BI, Brown DH (October 1965). "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. doi:10.1016/s0926-6593(65)80101-1. PMID 4286143.
- ^ Jeffrey PL, Brown DH, Brown BI (March 1970). "Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme". Biochemistry. 9 (6): 1403–15. doi:10.1021/bi00808a015. PMID 4313883.
- ^ Kelly JJ, Alpers DH (July 1973). "Properties of human intestinal glucoamylase". Biochimica et Biophysica Acta (BBA) - Enzymology. 315 (1): 113–22. doi:10.1016/0005-2744(73)90135-6. PMID 4743896.
- ^ Copeland WH, Miller KD (October 1956). "A blood trans-α-glucosylase". Biochimica et Biophysica Acta. 22 (1): 193–4. doi:10.1016/0006-3002(56)90242-6. PMID 13373867.
- ^ Tsujisaka Y, Fukumoto J, Yamamcto T (March 1958). "Specificity of crystalline saccharogenic amylase of moulds". Nature. 181 (4611): 770–1. Bibcode:1958Natur.181..770T. doi:10.1038/181770a0. PMID 13517301. S2CID 2810440.
External links
- Glucan+1,4-alpha-glucosidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This page was last edited on 26 August 2023, at 14:12