| Sucrose α-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.48 | ||||||||
| CAS no. | 37288-39-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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. [1] [2] [3] [4] [5] [6] 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)
| Sucrose α-glucosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.2.1.48 | ||||||||
| CAS no. | 37288-39-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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. [1] [2] [3] [4] [5] [6] 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)