Glukan 1,4-a-glukozidaza
| Glukan 1,4-a-glukozidaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Glukoamilaza homohexamer, Penicillium oxalicum | |||||||||
| Identifikatori | |||||||||
| EC broj | 3.2.1.3 | ||||||||
| CAS broj | 9032-08-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Glukan 1,4-a-glukozidaza (EC 3.2.1.3, glukoamilaza, amiloglukozidaza, gama-amilaza, lizozomalna alfa-glukozidaza, kiselinska maltaza, ekso-1,4-alfa-glukozidaza, glukozna amilaza, gama-1,4-glukanska glukohidrolaza, kiselinska maltaza, 1,4-alfa-D-glukanska glukohidrolaza) je enzim sa sistematskim imenom 4-alfa-D-glukan glukohidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- hidroliza terminalnih (1->4)-vezanih alfa-D-glukoznih ostataka sukcesivno sa neredukujućih krajeva lanaca uz oslobađanje beta-D-glukoza
Većina formi ovog enzima brzo hidrolizuje 1,6-alfa-D-glukozidne veze.
Reference
- ↑ French, D. and Knapp, D.W. (1950). „The maltase of Clostridium acetobutylicum”. J. Biol. Chem. 187: 463-471. PMID 14803428.
- ↑ Illingworth Brown, B. and Brown, D.H. (1965). „The subcellular distribution of enzymes in type II glycogenosis and the occurrence of an oligo-α-1,4-glucan glucohydrolase in human tissues”. Biochim. Biophys. Acta 110: 124-133. PMID 4286143.
- ↑ Jeffrey, P.L., Brown, D.H. and Brown, B.I. (1970). „Studies of lysosomal α-glucosidase. I. Purification and properties of the rat liver enzyme”. Biochemistry 9: 1403-1415. PMID 4313883.
- ↑ Kelly, J.J. and Alpers, D.H. (1973). „Properties of human intestinal glucoamylase”. Biochim. Biophys. Acta 315: 113-122. PMID 4743896.
- ↑ Miller, K.D. and Copeland, W.H. (1956). „A blood trans-α-glucosylase”. Biochim. Biophys. Acta 22: 193-194. PMID 13373867.
- ↑ Tsujisaka, Y., Fukimoto, J. and Yamamoto, T. (1958). „Specificity of crystalline saccharogenic amylase of moulds”. Nature 181: 770-771. PMID 13517301.
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 Glucan+1,4-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
