Agaraza
Agaraza (EC 3.2.1.81, AgaA, AgaB, endo-beta-agaraza, agarozna 3-glikanohidrolaza) je enzim sa sistematskim imenom agaroza 4-glikanohidrolaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Agaraza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 3.2.1.81 | ||||||||
| CAS broj | 37288-57-6 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
- hidroliza (1->4)-beta-D-galaktozidinih veza u agarozi, kojom se formira tetramer kao predominantni produkt
Ovaj enzim takođe deluje on porfiran.
Reference uredi
- ↑ Duckworth, M. and Turvey, J.R. (1969). „The action of a bacterial agarase on agarose, porphyran and alkali-treated porphyran”. Biochem. J. 113: 687-692. PMID 5386190.
- ↑ Allouch, J., Jam, M., Helbert, W., Barbeyron, T., Kloareg, B., Henrissat, B. and Czjzek, M. (2003). „The three-dimensional structures of two β-agarases”. J. Biol. Chem. 278: 47171-47180. PMID 12970344.
- ↑ Ohta, Y., Nogi, Y., Miyazaki, M., Li, Z., Hatada, Y., Ito, S. and Horikoshi, K. (2004). „Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from the novel marine isolate, JAMB-A94”. Biosci. Biotechnol. Biochem. 68: 1073-1081. PMID 15170112.
- ↑ Ohta, Y., Hatada, Y., Nogi, Y., Miyazaki, M., Li, Z., Akita, M., Hidaka, Y., Goda, S., Ito, S. and Horikoshi, K. (2004). „Enzymatic properties and nucleotide and amino acid sequences of a thermostable β-agarase from a novel species of deep-sea Microbulbifer”. Appl. Microbiol. Biotechnol. 64: 505-514. PMID 15088129.
- ↑ Sugano, Y., Terada, I., Arita, M., Noma, M. and Matsumoto, T. (1993). „Purification and characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107”. Appl. Environ. Microbiol. 59: 1549-1554. PMID 8517750.
- ↑ Jam, M., Flament, D., Allouch, J., Potin, P., Thion, L., Kloareg, B., Czjzek, M., Helbert, W., Michel, G. and Barbeyron, T. (2005). „The endo-β-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours”. Biochem. J. 385: 703-713. PMID 15456406.
Literatura uredi
- 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.