Ksantin oksidaza

(Preusmjereno sa stranice Ksantinska oksidaza)

Ksantin oksidaza (EC 1.17.3.2, hipoksantinska oksidaza, hipoksantin:kiseonik oksidoreduktaza, Schardinger enzim, ksantinska oksidoreduktaza, hipoksantin-ksantinska oksidaza, ksantin:O2 oksidoreduktaza, ksantin:ksantine oksidaza) je enzim sa sistematskim imenom ksantin:kiseonik oksidoreduktaza.[1][2][3][4][5][6][7][8][9][10] Ovaj enzim katalizuje sledeću hemijsku reakciju

Ksantin oksidaza
Identifikatori
EC broj 1.17.3.2
CAS broj 9002-17-9
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
ksantin + H2O + O2 urat + H2O2

Ovaj gvožđe-molibdenski flavoprotein (FAD) sadrži [2Fe-2S] centre. On takođe oksiduje hipoksantin, neke druge purine i pterine, i aldehide.

Reference uredi

  1. Avis, P.G., Bergel, F. and Bray, R.C. (1955). „Cellular constituents. The chemistry of xanthine oxidase. Part I. The preparation of a crystalline xanthine oxidase from cow's milk”. J. Chem. Soc. (Lond.): 1100-1105. 
  2. Battelli, M.G. and Lorenzoni, E. (1982). „Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver”. Biochem. J. 207: 133-138. PMID 6960894. 
  3. Bray, R.C. (1963). „Xanthine oxidase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 533-556. 
  4. Della Corte, E. and Stirpe, F. (1972). „The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzyme”. Biochem. J. 126: 739-745. PMID 4342395. 
  5. Ikegami, T. and Nishino, T. (1986). „The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver”. Arch. Biochem. Biophys. 247: 254-260. PMID 3459393. 
  6. Engerson, T.D., McKelvey, T.G., Rhyne, D.B., Boggio, E.B., Snyder, S.J. and Jones, H.P. (1987). „Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues”. J. Clin. Invest. 79: 1564-1570. PMID 3294898. 
  7. Saito, T., Nishino, T. and Tsushima, K. (1989). „Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them”. Adv. Exp. Med. Biol. 253B: 179-183. PMID 2610112. 
  8. Carpani, G., Racchi, M., Ghezzi, P., Terao, M. and Garattini, E. (1990). „Purification and characterization of mouse liver xanthine oxidase”. Arch. Biochem. Biophys. 279: 237-241. PMID 2350174. 
  9. Eger, B.T., Okamoto, K., Enroth, C., Sato, M., Nishino, T., Pai, E.F. and Nishino, T. (2000). „Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk”. Acta Crystallogr. D Biol. Crystallogr. 56: 1656-1658. PMID 11092937. 
  10. Nishino, T., Okamoto, K., Eger, B.T., Pai, E.F. and Nishino, T. (2008). „Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase”. FEBS J. 275: 3278-3289. PMID 18513323. 

Literatura uredi

  • Bray, R.C. (1963). „Xanthine oxidase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 533-556. 

Spoljašnje veze uredi