Sucrose α-glucosidase

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Sucrose α-glucosidase (EC 3.2.1.48, sucrose α-glucohydrolase, sucrase, sucrase-isomaltase, sucrose.α.-glucohydrolase, intestinal sucrase, sucrase(invertase)) is an enzyme with systematic name sucrose-α-D-glucohydrolase. It catalyses the hydrolysis of sucrose and maltose by an α-D-glucosidase-type action.

This enzyme is isolated from intestinal mucosa as a single polypeptide chain. The human sucrase-isomaltase is a dual-function enzyme with two GH31 domains, one serving as the isomaltase, the other serving as a sucrose α-glucosidase.

References

Conklin KA, Yamashiro KM, Gray GM (August 1975). "Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits". The Journal of Biological Chemistry. 250 (15): 5735–41. doi:10.1016/S0021-9258(19)41116-2. PMID 807575.
Hauri HP, Quaroni A, Isselbacher KJ (October 1979). "Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase". Proceedings of the National Academy of Sciences of the United States of America. 76 (10): 5183–6. doi:10.1073/pnas.76.10.5183. PMC 413104. PMID 291933.
Kolínská J, Kraml J (September 1972). "Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine". Biochimica et Biophysica Acta (BBA) - Enzymology. 284 (1): 235–47. doi:10.1016/0005-2744(72)90062-9. PMID 5073761.
Sigrist H, Ronner P, Semenza G (October 1975). "A hydrophobic form of the small-intestinal sucrase-isomaltase complex". Biochimica et Biophysica Acta (BBA) - Biomembranes. 406 (3): 433–46. doi:10.1016/0005-2736(75)90022-x. PMID 1182172.
Sjöström H, Norén O, Christiansen L, Wacker H, Semenza G (December 1980). "A fully active, two-active-site, single-chain sucrase.isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein". The Journal of Biological Chemistry. 255 (23): 11332–8. doi:10.1016/S0021-9258(19)70296-8. PMID 7002920.
Takesue Y (April 1969). "Purification and properties of rabbit intestinal sucrase". Journal of Biochemistry. 65 (4): 545–52. doi:10.1093/oxfordjournals.jbchem.a129048. PMID 5804876.

External links

Sucrose+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)

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EC 3.2.1