Saharoza alfa-glukozidaza
| Saharoza alfa-glukozidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.48 | ||||||||
| CAS broj | 37288-39-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Saharoza alfa-glukozidaza (EC 3.2.1.48, saharoza alfa-glukohidrolaza, sukraza, sukraza-izomaltaza, saharoza alfa-glukohidrolaza, intestinalna sukraza, sukraza (invertaza)) je enzim sa sistematskim imenom saharoza-alfa-D-glukohidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- hidroliza saharoze i maltoze na alfa-D-glukozidazni način
Ovaj enzim je izolovan iz intestinalnog mukusa kao samostalan polipeptidni lanac.
Reference
- ↑ Conklin, K.A., Yamashiro, K.M. and Gray, G.M. (1975). „Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits”. J. Biol. Chem. 250: 5735-5741. PMID 807575.
- ↑ Hauri, H.-P., Quaroni, A. and Isselbacher, K.J. (1979). „Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase”. Proc. Natl. Acad. Sci. USA 76: 5183-5186. PMID 291933.
- ↑ Kolinska, J. and Kraml, J. (1972). „Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine”. Biochim. Biophys. Acta 284: 235-247. PMID 5073761.
- ↑ Sigrist, H., Ronner, P. and Semenza, G. (1975). „A hydrophobic form of the small-intestinal sucrase-isomaltase complex”. Biochim. Biophys. Acta 406: 433-446. PMID 1182172.
- ↑ Sjöström, H., Norén, O., Christiansen, L., Wacker, H. and Semenza, G. (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”. J. Biol. Chem. 255: 11332-11338. PMID 7002920.
- ↑ Takesue, Y. (1969). „Purification and properties of rabbit intestinal sucrase”. J. Biochem. (Tokyo) 65: 545-552. PMID 5804876.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Spoljašnje veze
- MeSH Sucrose+alpha-glucosidase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
