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Gene Review

XDH  -  xanthine dehydrogenase

Gallus gallus

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Disease relevance of XDH


High impact information on XDH


Chemical compound and disease context of XDH


Biological context of XDH


Anatomical context of XDH

  • Markedly increasing levels of PNP and XDH were observed along with the enrichment in epithelial cells together with a slight, though significant, decrease in HGPRT activity [10].
  • By contrast, a dramatic fall in PNP and XDH activities was detected along with the enrichment in lymphocytes together with a slight, though significant, increase in HGPRT activity [10].
  • The results implied that high expression of PTPS is correlated with the biosynthesis of pteridines in the erythrophores and xanthophores, while the association between the putative guppy XDH with specific chromatophores is less clear [9].
  • Autoradiography of denaturing gels of xanthine dehydrogenase isolated from 32P(i)-labeled hepatocytes demonstrates that the 150-kDa and the 130-kDa forms of the enzyme are phosphorylated [8].
  • In response to a high protein diet the activity of cytosol 5'-nucleotidase in chicken liver increased, concurrently with those of purine nucleoside phosphorylase and xanthine dehydrogenase [11].

Associations of XDH with chemical compounds

  • Reduction of these enzymes by xanthine was limited at a rate comparable to that for the release of urate from native XDH [4].
  • There was no significant correlation between liver XDH activities and plasma uric acid levels; however, the activity was significantly higher in the HUA than in the LUA line [12].
  • On treatment with sodium dodecyl sulfate and 2-mercapto-ethanol, XDH was split into two subunits (named as alpha and beta) of different size in an equimolar ratio [13].
  • The mean value of kidney XDH activity was 85.41 +/- 13.81 and 46.35 +/- 6.71 mmoles NAD reduced per milligram acetone powder per hour, respectively, for the HUA and LUA lines [12].
  • Liver xanthine dehydrogenase (XDH) and kidney arginase were both increased even in the first stages of vitamin A deficiency [14].

Other interactions of XDH


Analytical, diagnostic and therapeutic context of XDH

  • Reductive titration with xanthine of native xanthine dehydrogenase in the presence of NAD showed that redox potentials of the FAD/FADH. and FADH./FADH2 couples were shifted positive by NAD binding to the enzyme [19].
  • Immunoprecipitated xanthine dehydrogenase from cell extracts migrates with enzyme purified from adult chicken liver on SDS/PAGE [8].
  • The present study describes the (xanthine:NAD+ oxidoreductase, EC synthesis and degradation of chick liver xanthine dehydrogenase in vivo and in organ cultures [20].


  1. Purification and characterization of a prokaryotic xanthine dehydrogenase from Comamonas acidovorans. Xiang, Q., Edmondson, D.E. Biochemistry (1996) [Pubmed]
  2. Identification of a molybdopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa. Johnson, J.L., Chaudhury, M., Rajagopalan, K.V. Biofactors (1991) [Pubmed]
  3. The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure. Sato, A., Nishino, T., Noda, K., Amaya, Y., Nishino, T. J. Biol. Chem. (1995) [Pubmed]
  4. Reactivity of chicken liver xanthine dehydrogenase containing modified flavins. Nishino, T., Nishino, T., Schopfer, L.M., Massey, V. J. Biol. Chem. (1989) [Pubmed]
  5. The reactivity of chicken liver xanthine dehydrogenase with molecular oxygen. Nishino, T., Nishino, T., Schopfer, L.M., Massey, V. J. Biol. Chem. (1989) [Pubmed]
  6. Differences in protein structure of xanthine dehydrogenase and xanthine oxidase revealed by reconstitution with flavin active site probes. Massey, V., Schopfer, L.M., Nishino, T., Nishino, T. J. Biol. Chem. (1989) [Pubmed]
  7. Kinetic comparison of reduction and intramolecular electron transfer in milk xanthine oxidase and chicken liver xanthine dehydrogenase by laser flash photolysis. Walker, M.C., Hazzard, J.T., Tollin, G., Edmondson, D.E. Biochemistry (1991) [Pubmed]
  8. Studies on the induction and phosphorylation of xanthine dehydrogenase in cultured chick embryo hepatocytes. Schieber, A., Edmondson, D.E. Eur. J. Biochem. (1993) [Pubmed]
  9. Cloning and tissue expression of 6-pyruvoyl tetrahydropterin synthase and xanthine dehydrogenase from Poecilia reticulata. Ben, J., Lim, T.M., Phang, V.P., Chan, W.K. Mar. Biotechnol. (2003) [Pubmed]
  10. Purine metabolism and B-lymphocyte development in the chicken bursa of fabricius. Senesi, S., Freer, G., Batoni, G., Barnini, S., Ghelardi, E., Bianchi, F., Dolfi, A., Lupetti, M., Campa, M. Dev. Comp. Immunol. (1992) [Pubmed]
  11. Properties of cytosol 5'-nucleotidase and its role in purine nucleotide metabolism. Tsushima, K. Adv. Enzyme Regul. (1986) [Pubmed]
  12. Purine metabolism studies in the high and low uric acid containing lines of chickens: de novo uric acid synthesis and xanthine dehydrogenase activities. McFarland, D.C., Coon, C.N. Poult. Sci. (1980) [Pubmed]
  13. Subunit constitution of electrophoretically purified xanthine dehydrogenase of avian liver. Irie, S. J. Biochem. (1984) [Pubmed]
  14. Influence of vitamin A on formation and excretion of end products of nitrogen catabolism in chicks. Bruckental, I., Ascarelli, I. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (1975) [Pubmed]
  15. Molybdopterin in carbon monoxide oxidase from carboxydotrophic bacteria. Meyer, O., Rajagopalan, K.V. J. Bacteriol. (1984) [Pubmed]
  16. Protein intake, hepatic purine enzyme levels and uric acid production in growing chicks. Hevia, P., Clifford, A.J. J. Nutr. (1978) [Pubmed]
  17. The influence of tungsten on the molybdenum status of poultry. Nell, J.A., Annison, E.F., Balnave, D. Br. Poult. Sci. (1980) [Pubmed]
  18. Amino-acid metabolism enzyme activities in the liver, intestine and yolk sac membrane of developing domestic fowl. Pons, A., García, F.J., Palou, A., Alemany, M. Arch. Int. Physiol. Biochim. (1986) [Pubmed]
  19. The nicotinamide adenine dinucleotide-binding site of chicken liver xanthine dehydrogenase. Evidence for alteration of the redox potential of the flavin by NAD binding or modification of the NAD-binding site and isolation of a modified peptide. Nishino, T., Nishino, T. J. Biol. Chem. (1989) [Pubmed]
  20. Synthesis and degradation of xanthine dehydrogenase in chick liver. In vivo and in vitro studies. Thompson, J.M., Nickels, J.S., Fisher, J.R. Biochim. Biophys. Acta (1979) [Pubmed]
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