Alfa-D-ksilozid ksilohidrolaza
| Alfa-D-ksilozid ksilohidrolaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.177 | ||||||||
| 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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Alfa-D-ksilozid ksilohidrolaza (EC 3.2.1.177, alfa-ksilozidaza) je enzim sa sistematskim imenom alfa-D-ksilozid ksilohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- hidroliza terminalnih, neredukujućih alfa-D-ksiloznih ostataka uz otpuštanje alfa-D-ksiloze
Ovaj enzim katalizuje hidrolizu terminalnog, nesupstituisanog ksilozida na redukujućem kraju ksilogluko-oligosaharida.
- ↑ Moracci, M., Cobucci Ponzano, B., Trincone, A., Fusco, S., De Rosa, M., van Der Oost, J., Sensen, C.W., Charlebois, R.L. and Rossi, M. (2000). „Identification and molecular characterization of the first α -xylosidase from an archaeon”. J. Biol. Chem. 275: 22082-22089. PMID 10801892.
- ↑ Sampedro, J., Sieiro, C., Revilla, G., Gonzalez-Villa, T. and Zarra, I. (2001). „Cloning and expression pattern of a gene encoding an α-xylosidase active against xyloglucan oligosaccharides from Arabidopsis”. Plant Physiol. 126: 910-920. PMID 11402218.
- ↑ Crombie, H.J., Chengappa, S., Jarman, C., Sidebottom, C. and Reid, J.S. (2002). „Molecular characterisation of a xyloglucan oligosaccharide-acting α-D-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant ’apoplastic’ α-D-glucosidases”. Planta 214: 406-413. PMID 11859845.
- ↑ Lovering, A.L., Lee, S.S., Kim, Y.W., Withers, S.G. and Strynadka, N.C. (2005). „Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate”. J. Biol. Chem. 280: 2105-2115. PMID 15501829.
- ↑ Iglesias, N., Abelenda, J.A., Rodino, M., Sampedro, J., Revilla, G. and Zarra, I. (2006). „Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana”. Plant Cell Physiol. 47: 55-63. PMID 16267099.
- ↑ Okuyama, M., Kaneko, A., Mori, H., Chiba, S. and Kimura, A. (2006). „Structural elements to convert Escherichia coli α-xylosidase (YicI) into α-glucosidase”. FEBS Lett. 580: 2707-2711. PMID 16631751.
- ↑ Larsbrink, J., Izumi, A., Ibatullin, F., Nakhai, A., Gilbert, H.J., Davies, G.J. and Brumer, H. (2011). „Structural and enzymatic characterisation of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification”. Biochem. J. 436: 567-580. PMID 21426303.
- 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.