Class 1 · Oxidoreductases pp 674-718 | Cite as
Xanthine dehydrogenase
Chapter
Keywords
Methylene Blue Xanthine Oxidase Nitroblue Tetrazolium Methyl Viologen Xanthine Dehydrogenase
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Preview
Unable to display preview. Download preview PDF.
References
- [1]Battelli, M.G.; Lorenzoni, E.: Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J., 207, 133–138 (1982)PubMedGoogle Scholar
- [2]Eger, B.T.; Okamoto, K.; Enroth, C.; Sato, M.; Nishino, T.; Pai, E.F.; Nishino, T.: Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk. Acta Crystallogr. Sect. D, 56, 1656–1658 (2000)CrossRefGoogle Scholar
- [3]Bruguera, P.; Lopez-Cabrera, A.; Canela, E.I.: Kinetic mechanism of chicken liver xanthine dehydrogenase. Biochem. J., 249, 171–178 (1988)PubMedGoogle Scholar
- [4]Wajner, M.; Harkness, R.A.: Distribution of xanthine dehydrogenase and oxidase activities in human and rabbit tissues. Biochem. Soc. Trans., 16, 358–359 (1988)Google Scholar
- [5]Wajner, M.; Harkness, R.A.: Distribution of xanthine dehydrogenase and oxidase activities in human and rabbit tissues. Biochim. Biophys. Acta, 991, 79–84 (1989)PubMedGoogle Scholar
- [6]Stark, K.; Seubert, P.; Lynch, G.; Baudry, M.: Proteolytic conversion of xanthine dehydrogenase to xanthine oxidase: Evidence against a role for calcium-activated protease (calpain). Biochem. Biophys. Res. Commun., 165, 858–864 (1989)PubMedCrossRefGoogle Scholar
- [7]Adams, B.; Lowe, D.J.; Smith, A.T.; Scazzocchio, C.; Demais, S.; Bray, R.C.: Expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans and some properties of the recombinant enzyme. Biochem. J., 362, 223–229 (2002)PubMedCrossRefGoogle Scholar
- [8]Kim, J.M.; Schmid, R.D.: Purification and characterization of a microbial xanthine dehydrogenase highly active towards hypoxanthine. GBF Monogr., Biosens. Appl. Med., Environ. Prot. Process Control, 13, 421–424 (1989)Google Scholar
- [9]Parschat, K.; Canne, C.; Huttermann, J.; Kappl, R.; Fetzner, S.: Xanthine dehydrogenase from Pseudomonas putida 86: Specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization. Biochim. Biophys. Acta, 1544, 151–165 (2001)PubMedGoogle Scholar
- [10]Morita, Y.; Sawada, M.; Seno, H.; Takaishi, S.; Fukutawa, H.; Miyake, N.; Hiai, H.; Chiba, T.: Identification of xanthine dehydrogenase/xanthine oxidase as a rat paneth cell zinc-binding protein. Biochim. Biophys. Acta, 1540, 43–49 (2001)PubMedCrossRefGoogle Scholar
- [11]Enroth, C.; Eger, B.T.; Okamoto, K.; Nishino, T.; Nishino, T.; Pai, E.F.: Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion. Proc. Natl. Acad. Sci. USA, 97, 10723–10728 (2000)PubMedCrossRefGoogle Scholar
- [12]McManaman, J.L.; Neville, M.C.; Wright, R.M.: Mouse mammary gland xanthine oxidoreductase: Purification, characterization, and regulation. Arch. Biochem. Biophys., 371, 308–316 (1999)PubMedCrossRefGoogle Scholar
- [13]Schräder, T.; Rienhöfer, A.; Andreesen, J.R.: Selenium-containing xanthine dehydrogenase from Eubacterium barkeri. Eur. J. Biochem., 264, 862–871 (1999)PubMedCrossRefGoogle Scholar
- [14]Ichimori, K.; Fukahori, M.; Nakazawa, H.; Okamoto, K.; Nishino, T.: Inhibition of xanthine oxidase and xanthine dehydrogenase by nitric oxid. J. Biol. Chem., 274, 7763–7768 (1999)PubMedCrossRefGoogle Scholar
- [15]Montalbini, P.: Purification and some properties of xanthine dehydrogenase from wheat leaves. Plant Sci., 134, 89–102 (1998)CrossRefGoogle Scholar
- [16]Christiansen, L.C.; Schou, S.; Nygaard, P.; Saxild, H.H.: Xanthine metabolism in Bacillus subtilis: Characterization of the xpt-pbuX operon and evidence for purine-and nitrogen-controlled expression of genes involved in the xanthine salvage and catabolism. J. Bacteriol., 179, 2540–2550 (1997)PubMedGoogle Scholar
- [17]Gremer, L.; Meyer, O.: Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor. Eur. J. Biochem., 238, 862–866 (1996)PubMedCrossRefGoogle Scholar
- [18]Suleiman, S.A.; Stevens, J.B.: Purification of xanthine dehydrogenase from rat liver: A rapid procedure with high enzyme yields. Arch. Biochem. Biophys., 258, 219–225 (1987)PubMedCrossRefGoogle Scholar
- [19]Irie, S.: Subunit constitution of electrophoretically purified xanthine dehydrogenase of avian liver. J. Biochem., 95, 405–412 (1984)PubMedGoogle Scholar
- [20]Prez-Vicente, R.; Pineda, M.; Cardenas, J.: Occurrence of an NADH diaphorase activity associated with xanthine dehydrogenase in Chlamydomonas reinhardtii. FEMS Microbiol. Lett., 43, 321–325 (1987)Google Scholar
- [21]Fhaolain, I.N.; Coughlan, M.P.: Effects of limited proteolysis on the structure and activity of turkey liver xanthine dehydrogenase. Biochem. Soc. Trans., 5, 1705–1707 (1977)PubMedGoogle Scholar
- [22]Rocher-Chambonnet, C.; Berreur, P.; Houde, M.; Tiveron, M.C.; Lepesant, J.A.; Bregegere, F.: Cloning and partial characterization of the xanthine dehydrogenase gene of Calliphora vicina, a distant relative of Drosophila melanogaster. Gene, 59, 201–212 (1987)PubMedCrossRefGoogle Scholar
- [23]Schopfer, L.M.; Massey, V.; Nishino, T.: Rapid reaction studies on the reduction and oxidation of chicken liver xanthine dehydrogenase by the xanthine/urate and NAD/NADH couples. J. Biol. Chem., 263, 13528–13538 (1988)PubMedGoogle Scholar
- [24]Self, W.T.; Stadtman, T.C.: Selenium-dependent metabolism of purines: A selenium-dependent purine hydroxylase and xanthine dehydrogenase were purified from Clostridium purinolyticum and characterized. Proc. Natl. Acad. Sci. USA, 97, 7208–7213 (2000)PubMedCrossRefGoogle Scholar
- [25]Hughes, R.K.; Doyle, W.A.; Chovnick, A.; Whittle, J.R.S.; Burke, J.F.; Bray, R.C.: Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase. Biochem. J., 285, 507–513 (1992)PubMedGoogle Scholar
- [26]Rajagopalan, K.V.; Handler, P.: Purification and properties of chicken liver xanthine dehydrogenase. J. Biol. Chem., 242, 4097–4107 (1967)PubMedGoogle Scholar
- [27]Waud, W.R.; Rajagopalan, K.V.: Purification and properties of the NAD+-dependent (type D) and O2-dependent (type O) forms of rat liver xanthine dehydrogenase. Arch. Biochem. Biophys., 172, 354–364 (1976)PubMedCrossRefGoogle Scholar
- [28]Sin, I.L.: Purification and properties of xanthine dehydrogenase from Pseudomonas acidovorans. Biochim. Biophys. Acta, 410, 12–20 (1975)PubMedGoogle Scholar
- [29]Della Corte, E.; Stirpe, F.: 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 (1972)PubMedGoogle Scholar
- [30]Xiang, Q.; Edmondson, D.E.: Purification and characterization of a prokaryotic xanthine dehydrogenase from Comamonas acidovorans. Biochemistry, 35, 5441–5450 (1996)PubMedCrossRefGoogle Scholar
- [31]Doyle, W.A.; Burke, J.F.; Chovnick, A.; Dutton, F.L.; Whittle, J.R.S.; Bray, R.C.: Properties of xanthine dehydrogenase variants from rosy mutant strains of Drosophila melanogaster and their relevance to the enzyme’s structure and mechanism. Eur. J. Biochem., 239, 782–795 (1996)PubMedCrossRefGoogle Scholar
- [32]Wright, R.M.; Vaitaitis, G.M.; Wilson, C.M.; Repine, T.B.; Terada, L.S.; Repine, J.E.: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc. Natl. Acad. Sci. USA, 90, 10690–10694 (1993)PubMedCrossRefGoogle Scholar
- [33]Leydecker, M.T.; Moureaux, T.; Kraepiel, Y.; Schnorr, K.; Caboche, M.: Molybdenum cofactor mutants, specifically impaired in xanthine dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase. Plant Physiol., 107, 1427–1431 (1995)PubMedGoogle Scholar
- [34]Waud, W.R.; Rajagopalan, K.V.: The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an O2-dependent form (type O). Arch. Biochem. Biophys., 172, 365–379 (1976)PubMedCrossRefGoogle Scholar
- [35]Hunt, J.; Massey, V.: Purification and properties of milk xanthine dehydrogenase. J. Biol. Chem., 267, 21479–21485 (1992)PubMedGoogle Scholar
- [36]Nguyen, J.; Feierabend, J.: Some properties and subcellular localization of xanthine dehydrogenase in pea leaves. Plant Sci. Lett., 13, 125–132 (1978)CrossRefGoogle Scholar
- [37]Perez-Vicente, R.; Alamillo, J.M.; Cardenas, J.; Pineda, M.: Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtii. Biochim. Biophys. Acta, 1117, 159–166 (1992)PubMedGoogle Scholar
- [38]Panus, P.C.; Burgess, B.; Freeman, B.A.: Characterization of cultured alveolar epithelial cell xanthine dehydrogenase/oxidase. Biochim. Biophys. Acta, 1091, 303–309 (1991)PubMedCrossRefGoogle Scholar
- [39]Wagner, R.; Cammack, R.; Andreesen, J.R.: Purification and characterization of xanthine dehydrogenase from Clostridium acidiurici grown in the presence of selenium. Biochim. Biophys. Acta, 791, 63–74 (1984)Google Scholar
- [40]Woolfolk, C.A.: Purification and properties of a novel ferricyanide-linked xanthine dehydrogenase from Pseudomonas putida 40. J. Bacteriol., 163, 600–609 (1985)PubMedGoogle Scholar
- [41]Woolfolk, C.A.; Downard, J.S.: Distribution of xanthine oxidase and xanthine dehydrogenase specificity types among bacteria. J. Bacteriol., 130, 1175–1191 (1977)PubMedGoogle Scholar
- [42]Yen, T.T.T.; Glassman, E.: Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster: II. Enzyme kinetics. Biochim. Biophys. Acta, 146, 35–44 (1967)PubMedGoogle Scholar
- [43]Seybold, W.D.: Purification and partial characterization of xanthine dehydrogenase from Drosophila melanogaster. Biochim. Biophys. Acta, 334, 266–271 (1974)Google Scholar
- [44]Smith, S.T.; Rajagopalan, K.V.; Handler, P.: Purification and properties of xanthine dehydrogenase from Micrococcus lactilyticus. J. Biol. Chem., 242, 4108–4117 (1967)PubMedGoogle Scholar
- [45]Hughes, R.K.; Bennett, B.; Bray, R.C.: Xanthine dehydrogenase from Drosophila melanogaster: Purification and properties of the wild-type enzyme and of a variant lacking iron-sulfur centers. Biochemistry, 31, 3073–3083 (1992)PubMedCrossRefGoogle Scholar
- [46]Kaminski, Z.W.; Jezewska, M.M.: Effect of NADH on hypoxanthine hydroxylation by native NAD+-dependent xanthine oxidoreductase of rat liver, and the possible biological role of this effect. Biochim. J., 200, 597–603 (1981)Google Scholar
- [47]Kaminsky, Z.W.; Jezewska, M.M.: Involvement of a single thiol group in the conversion of the NAD+-dependent activity of rat liver xanthine oxidore-ductase to the O2-dependent activity. Biochem. J., 207, 341–346 (1982)Google Scholar
- [48]Topham, R.W.; Walker, M.C.; Calisch, M.: Liver xanthine dehydrogenase and iron mobilization. Biochem. Biophys. Res. Commun., 109, 1240–1246 (1982)PubMedCrossRefGoogle Scholar
- [49]Triplett, E. W.; Blevins, D.G.; Randall, D.D.: Purification and properties of soybean nodule xanthine dehydrogenase. Arch. Biochem. Biophys., 219, 39–46 (1982)PubMedCrossRefGoogle Scholar
- [50]Truglio, J.J.; Theis, K.; Leimkuhler, S.; Rappa, R.; Rajagopalan, K.V.; Kisker, C.: Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. Structure, 10, 115–125 (2002)PubMedCrossRefGoogle Scholar
- [51]Lyon, E.S.; Garrett, R.H.: Regulation, purification, and properties of xanthine dehydrogenase in Neurospora crassa. J. Biol. Chem., 253, 2604–2614 (1978)PubMedGoogle Scholar
- [52]Parzen, S.D.; Fox, A.S.: Purification of xanthine dehydrogenase from Drosophila melanogaster. Biochim. Biophys. Acta, 92, 465–471 (1964)PubMedGoogle Scholar
- [53]Coolbear, K.P.; Herzberg, G.R.; Brosnan, J.T.: Xanthine dehydrogenase in chicken liver: Its subcelluar localization ant its possible role on gluconeogenesis from amino acids. Biochem. Soc. Trans., 9, 394–395 (1981)Google Scholar
- [54]Watt, W.B.: Xanthine dehydrogenase and pteridine metabolism in Colias butterflies. J. Biol. Chem., 247, 1445–1451 (1972)PubMedGoogle Scholar
- [55]Aretz, W.; Kaspari, H.; Klemme, J.H.: Molecular and kinetic characterization of xanthine dehydrogenase from the phototrophic bacterium Rodopseudomonas capsulata. Z. Naturforsch. C, 36, 933–941 (1981)Google Scholar
- [56]Boland, M.J.; Blevins, D.G.; Randall, D.D.: Soybean nodule xanthine dehydrogenase: A kinetic study. Arch. Biochem. Biophys., 222, 435–441 (1983)PubMedCrossRefGoogle Scholar
- [57]Edwards, T.C.R.; Candido, E.P.M.: Xanthine dehydrogenase from Drosophila melanogaster. A comparison of the kinetic parameters of the pure enzyme from two wild-type isoalleles differing at a putative regulatory site. Mol. Gen. Genet., 154, 1–6 (1977)PubMedCrossRefGoogle Scholar
- [58]Fernandez, E.; Cardenas, J.: Occurrence of xanthine dehydrogenase in Chlamydomonas reinhardii: A common cofactor shared by xanthine dehydrogenase and nitrate reductase. Planta, 153, 254–257 (1981)CrossRefGoogle Scholar
- [59]Tramper, J.; Angelino, S.A.G.F.; Muller, F.; van der Plas, H.C.: Kinetics and stability of immobilized chicken liver xanthine dehydrogenase. Biotechnol. Bioeng., 21, 1767–1786 (1979)PubMedCrossRefGoogle Scholar
- [60]Wagner, R.; Andreesen, J.R.: Selenium requirement for active xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum. Arch. Microbiol., 121, 255–260 (1979)PubMedCrossRefGoogle Scholar
- [61]Coughlan, M.P.; Johnson, D.B.: The inactivation of xanthine-oxidizing enzymes, native and deflavo forms, in the presence of oxygen. Biochem. Soc. Trans., 7, 18–21 (1979)PubMedGoogle Scholar
- [62]Ohe, T.; Watanabe, Y.: Purification and properties of xanthine dehydrogenase from Streptomyces cyanogenus. J. Biochem., 86, 45–53 (1979)PubMedGoogle Scholar
- [63]Sakai, T.; Jun, H.K.: Purification, crystallization, and some properties of xanthine dehydrogenase from Pseudomonas synxantha A 3. Agric. Biol. Chem., 43, 753–760 (1979)Google Scholar
- [64]Nakamura, M.; Yamazaki, I.: Preparation of bovine milk xanthine oxidase as a dehydrogenase form. J. Biochem., 92, 1279–1286 (1982)PubMedGoogle Scholar
- [65]Taylor, N.J.; Cowan, A.K.: Xanthine dehydrogenase and aldehyde oxidase impact plant hormone homeostasis and affect fruit size in ‘Hass’ avocado. J. Plant Res., 177, 121–130 (2004)Google Scholar
- [66]Frederiks, W.M.; Vreeling-Sindelarova, H.: Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells. Acta Histochem., 104, 29–37 (2002)PubMedCrossRefGoogle Scholar
- [67]Baghiani, A.; Harrison, R.; Benboubetra, M.: Purification and partial characterisation of camel milk xanthine oxidoreductase. Arch. Physiol. Biochem., 111, 407–414 (2003)PubMedCrossRefGoogle Scholar
- [68]Ivanov, N.V.; Hubalek, F.; Trani, M.; Edmondson, D.E.: Factors involved in the assembly of a functional molybdopyranopterin center in recombinant Comamonas acidovorans xanthine dehydrogenase. Eur. J. Biochem., 270, 4744–4754 (2003)PubMedCrossRefGoogle Scholar
- [69]Self, W.T.: Regulation of purine hydroxylase and xanthine dehydrogenase from Clostridium purinolyticum in response to purines, selenium, and molybdenum. J. Bacteriol., 184, 2039–2044 (2002)PubMedCrossRefGoogle Scholar
- [70]Nishino, T.; Amaya, Y.; Kawamoto, S.; Kashima, Y.; Okamoto, K.: Purification and characterization of multiple forms of rat liver xanthine oxidore-ductase expressed in baculovirus-insect cell system. J. Biochem., 132, 597–606 (2002)PubMedGoogle Scholar
- [71]Okamoto, K.; Eger, B.T.; Nishino, T.; Kondo, S.; Pai, E.F.: An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition. J. Biol. Chem., 278, 1848–1855 (2003)PubMedCrossRefGoogle Scholar
- [72]Leimkuhler, S.; Hodson, R.; George, G.N.; Rajagopalan, K.V.: Recombinant Rhodobacter capsulatus xanthine dehydrogenase, a useful model system for the characterization of protein variants leading to xanthinuria I in humans. J. Biol. Chem., 278, 20802–20811 (2003)PubMedCrossRefGoogle Scholar
- [73]Hesberg, C.; Hansch, R.; Mendel, R.R.; Bittner, F.: Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities. J. Biol. Chem., 279, 13547–13554 (2004)PubMedCrossRefGoogle Scholar
- [74]Leimkuhler, S.; Stockert, A.L.; Igarashi, K.; Nishino, T.; Hille, R.: The role of active site glutamate residues in catalysis of Rhodobacter capsulatus xanthine dehydrogenase. J. Biol. Chem., 279, 40437–40444 (2004)PubMedCrossRefGoogle Scholar
- [75]Nishino, T.; Okamoto, K.; Kawaguchi, Y.; Hori, H.; Matsumura, T.; Eger, B.T.; Pai, E.F.: Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant. J. Biol. Chem., 280, 24888–24894 (2005)PubMedCrossRefGoogle Scholar
- [76]Benboubetra, M.; Baghiani, A.; Atmani, D.; Harrison, R.: Physicochemical and kinetic properties of purified sheep’s milk xanthine oxidoreductase. J. Dairy Sci., 87, 1580–1584 (2004)PubMedCrossRefGoogle Scholar
- [77]Yesbergenova, Z.; Yang, G.; Oron, E.; Soffer, D.; Fluhr, R.; Sagi, M.: The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid. Plant J., 42, 862–876 (2005)PubMedCrossRefGoogle Scholar
- [78]Sauer, P.; Frebortova, J.; Sebela, M.; Galuszka, P.; Jacobsen, S.; Pec, P.; Frebort, I.: Xanthine dehydrogenase of pea seedlings: a member of the plant molybdenum oxidoreductase family. Plant Physiol. Biochem., 40, 393–400 (2002)CrossRefGoogle Scholar
- [79]Okamoto, K.; Matsumoto, K.; Hille, R.; Eger, B.T.; Pai, E.F.; Nishino, T.: The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition. Proc. Natl. Acad. Sci. USA, 101, 7931–7936 (2004)PubMedCrossRefGoogle Scholar
- [80]Ivanov, N.V.; Trani, M.; Edmondson, D.E.: High-level expression and characterization of a highly functional Comamonas acidovorans xanthine dehydrogenase in Pseudomonas aeruginosa. Protein Expr. Purif., 37, 72–82 (2004)PubMedCrossRefGoogle Scholar
- [81]Joshi, M.S.; Rajagopalan, K.V.: Specific incorporation of molybdopterin in xanthine dehydrogenase of Pseudomonas aeruginosa. Arch. Biochem. Biophys., 308, 331–334 (1994)PubMedCrossRefGoogle Scholar
- [82]Johnson, J.L.; Chaudhury, M.; Rajagopalan, K.V.: Identification of a molyb-dopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa. BioFactors, 3, 103–107 (1991)PubMedGoogle Scholar
- [83]Abdulnour, R.E.; Peng, X.; Finigan, J.H.; Han, E.J.; Hasan, E.J.; Birukov, K.G.; Reddy, S.P.; Watkins, J.E.; Kayyali, U.S.; Garcia, J.G.; Tuder, R.M.; Hassoun, P.M.: Mechanical stress activates xanthine oxidoreductase through MAP kinase-dependent pathways. Am. J. Physiol. Lung Cell Mol. Physiol., 291, L345–L353 (2006)PubMedCrossRefGoogle Scholar
- [84]Godber, B.L.; Schwarz, G.; Mendel, R.R.; Lowe, D.J.; Bray, R.C.; Eisenthal, R.; Harrison, R.: Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres. Biochem. J., 388, 501–508 (2005)PubMedCrossRefGoogle Scholar
- [85]Cheung, K.J.; Tzameli, I.; Pissios, P.; Rovira, I.; Gavrilova, O.; Ohtsubo, T.; Chen, Z.; Finkel, T.; Flier, J.S.; Friedman, J.M.: Xanthine oxidoreductase is a regulator of adipogenesis and PPARγ activity. Cell Metab., 5, 115–128 (2007)PubMedCrossRefGoogle Scholar
- [86]Maia, L.; Vala, A.; Mira, L.: NADH oxidase activity of rat liver xanthine dehydrogenase and xanthine oxidase-contribution for damage mechanisms. Free Radic. Res., 39, 979–986 (2005)PubMedCrossRefGoogle Scholar
- [87]Atmani, D.; Baghiani, A.; Harrison, R.; Benboubetra, M.: NADH oxidation and superoxide production by caprine milk xanthine oxidoreductase. Int. Dairy J., 15, 1113–1121 (2005)CrossRefGoogle Scholar
- [88]Yamaguchi, Y.; Matsumura, T.; Ichida, K.; Okamoto, K.; Nishino, T.: Human Xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate. J. Biochem., 141, 513–524 (2007)PubMedCrossRefGoogle Scholar
- [89]Asai, R.; Nishino, T.; Matsumura, T.; Okamoto, K.; Igarashi, K.; Pai, E.F.; Nishino, T.: Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase. J. Biochem., 141, 525–534 (2007)PubMedCrossRefGoogle Scholar
- [90]Neumann, M.; Schulte, M.; Juenemann, N.; Stoecklein, W.; Leimkuehler, S.: Rhodobacter capsulatus XdhC is involved in molybdenum cofactor binding and insertion into xanthine dehydrogenase. J. Biol. Chem., 281, 15701–15708 (2006)PubMedCrossRefGoogle Scholar
- [91]Pauff, J.M.; Hemann, C.F.; Juenemann, N.; Leimkuehler, S.; Hille, R.: The role of arginine 310 in catalysis and substrate specificity in xanthine dehydrogenase from Rhodobacter capsulatus. J. Biol. Chem., 282, 12785–12790 (2007)PubMedCrossRefGoogle Scholar
- [92]Roberts, L.E.; Fini, M.A.; Derkash, N.; Wright, R.M.: PD98059 enhanced insulin, cytokine, and growth factor activation of xanthine oxidoreductase in epithelial cells involves STAT3 and the glucocorticoid receptor. J. Cell. Biochem., 101, 1567–1587 (2007)PubMedCrossRefGoogle Scholar
- [93]Zhao, X.; Zhu, J.X.; Mo, S.F.; Pan, Y.; Kong, L.D.: Effects of cassia oil on serum and hepatic uric acid levels in oxonate-induced mice and xanthine dehydrogenase and xanthine oxidase activities in mouse liver. J. Ethnopharmacol., 103, 357–365 (2006)PubMedCrossRefGoogle Scholar
Copyright information
© Springer-Verlag Berlin Heidelberg 2009