Glucan 1,4-α-glucosidase - Misplaced Pages

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. 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.

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)

Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases

Disaccharidase	Sucrase/Sucrase-isomaltase/Invertase Maltase Trehalase Lactase
Glucosidases	Cellulase Alpha-glucosidase Acid Neutral AB Neutral C Beta-glucosidase cytosolic Debranching enzyme
Other	Amylase Alpha-amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha-Mannosidase Glucuronidase Klotho Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha-N-acetylgalactosaminidase NAGA Alpha-N-acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase-glucoamylase Heparanase HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds

DNA glycosylases: Oxoguanine glycosylase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Portal:

Biology

Category:

EC 3.2.1

See also

References

External links