Celulaza
| Celuloza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| Identifikatori | |||||||||
| EC broj | 3.2.1.4 | ||||||||
| CAS broj | 9012-54-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Celuloza (EC 3.2.1.4, endo-1,4-beta-D-glukanaza, beta-1,4-glukanaza, beta-1,4-endoglukanska hidrolaza, celulaza A, celulozin AP, endoglukanaza D, alkalna celulaza, celulaza A 3, celudekstrinaza, 9.5 celulaza, avicelaza, pancelaza SS, 1,4-(1,3, 1,4)-beta-D-glukan 4-glukanohidrolaza) je enzim sa sistematskim imenom 4-beta-D-glukan 4-glukanohidrolaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
Ovaj enzim hidrolizuje i 1,4-veze beta-D-glukana koji takođe sadrže 1,3-veze.
- ↑ Datta, P.K., Hanson, K.R. and Whitaker, D.R. (1963). „Improved procedures for preparation and characterization of Myrothecum cellulase. III. Molecular weight, amino acid composition, terminal residues, and other properties”. Can. J. Biochem. Physiol. 41: 697-705. PMID 14025219.
- ↑ Larner, J. (1960). „Other glucosidases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 4 (2nd izd.). New York: Academic Press. str. 369-378.
- ↑ Myers, F.L. and Northcote, D.H. (1959). „Partial purification and some properties of a cellulase from Helix pomatia”. Biochem. J. 71: 749-756. PMID 13651124.
- ↑ Nishizawa, K. and Hashimoto, Y. (1959). „Cellulose splitting enzymes. VI. Difference in the specificities of cellulase and β-glucosidase from Irpex lacteus”. Arch. Biochem. Biophys. 81: 211-222.
- ↑ Whitaker, D.R., Hanson, K.R. and Datta, P.K. (1963). „Improved procedures for preparation and characterization of myrothecium cellulase. 2. Purification procedures”. Can. J. Biochem. Physiol. 41: 671-696. PMID 14000266.
- ↑ Hatfield, R. and Nevins, D.J. (1986). „Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings”. Carbohydr. Res. 148: 265-278.
- ↑ Hatfield, R. and Nevins, D.J. (1987). „Hydrolytic activity and substrate specificity of an endoglucanase from Zea mays seedling cell walls”. Plant Physiol. 83: 203-207. PMID 16665203.
- ↑ Inohue, M., Hayashgi, K. and Nevins, D.J. (1999). „Polypeptide characteristics and immunological properties of exo- and endoglucanases purified from maize coleoptile cell walls”. J. Plant Physiol. 154: 334-340.
- 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.
- Larner, J. (1960). „Other glucosidases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 4 (2nd izd.). New York: Academic Press. str. 369-378.