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Agaraza

Izvor: Wikipedija
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

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

hidroliza (1->4)-beta-D-galaktozidinih veza u agarozi, kojom se formira tetramer kao predominantni produkt

Ovaj enzim takođe deluje on porfiran.

Reference

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  1. 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. 
  2. 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. 
  3. 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. 
  4. 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. 
  5. 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. 
  6. 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

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Vanjske veze

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