Ksantin oksidaza

Ksantin oksidaza
Identifikatori
EC broj1.17.3.2
CAS broj9002-17-9
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

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 + 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

  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. & 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”. Ур.: Boyer, P.D., Lardy, H.; Myrb; auml; ck, K. The Enzymes. 7 (2nd изд.). New York: Academic Press. стр. 533—556. 
  4. ^ Della Corte, E. & 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. & 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. 

Литература

  • Bray, R.C. (1963). „Xanthine oxidase”. Ур.: Boyer, P.D., Lardy, H.; Myrb; auml; ck, K. The Enzymes. 7 (2nd изд.). New York: Academic Press. стр. 533—556. 

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