| Entry |
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| Name |
xanthine dehydrogenase;
NAD+-xanthine dehydrogenase;
xanthine-NAD+ oxidoreductase;
xanthine/NAD+ oxidoreductase;
xanthine oxidoreductase
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| Class |
Oxidoreductases;
Acting on CH or CH2 groups;
With NAD+ or NADP+ as acceptor
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| Sysname |
xanthine:NAD+ oxidoreductase
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| Reaction(IUBMB) |
xanthine + NAD+ + H2O = urate + NADH + H+ [RN: R02103]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
Acts on a variety of purines and aldehydes, including hypoxanthine. The mammalian enzyme can also convert all-trans retinol to all-trans-retinoate, while the substrate is bound to a retinoid-binding protein [14]. The enzyme from eukaryotes contains [2Fe-2S], FAD and a molybdenum centre. The mammalian enzyme predominantly exists as the NAD-dependent dehydrogenase (EC 1.17.1.4). During purification the enzyme is largely converted to an O2-dependent form, xanthine oxidase (EC 1.17.3.2). The conversion can be triggered by several mechanisms, including the oxidation of cysteine thiols to form disulfide bonds [2,6,8,15] [which can be catalysed by EC 1.8.4.7, enzyme-thiol transhydrogenase (glutathione-disulfide) in the presence of glutathione disulfide] or limited proteolysis, which results in irreversible conversion. The conversion can also occur in vivo [2,7,15].
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| History |
EC 1.17.1.4 created 1972 as EC 1.2.1.37, transferred 1984 to EC 1.1.1.204, modified 1989, transferred 2004 to EC 1.17.1.4, modified 2011
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| Pathway |
| ec01120 | Microbial metabolism in diverse environments |
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| Orthology |
| K00087 | xanthine dehydrogenase molybdenum-binding subunit |
| K00106 | xanthine dehydrogenase/oxidase |
| K11177 | xanthine dehydrogenase YagR molybdenum-binding subunit |
| K11178 | xanthine dehydrogenase YagS FAD-binding subunit |
| K13479 | xanthine dehydrogenase FAD-binding subunit |
| K13481 | xanthine dehydrogenase small subunit |
| K13482 | xanthine dehydrogenase large subunit |
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| Genes |
» show all
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| Reference |
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| Authors |
Battelli MG, Lorenzoni E. |
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| Title |
Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. |
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| Journal |
Biochem J 207:133-8 (1982) |
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| Reference |
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| Authors |
Corte ED, Stirpe F. |
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| Title |
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. |
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| Journal |
Biochem J 126:739-45 (1972) |
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| Reference |
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| Authors |
PARZEN SD, FOX AS. |
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| Title |
PURIFICATION OF XANTHINE DEHYDROGENASE FROM DROSOPHILA MELANOGASTER. |
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| Journal |
Biochim Biophys Acta 92:465-71 (1964) |
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| Reference |
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| Authors |
Rajagopalan KV, Handler P. |
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| Title |
Purification and properties of chicken liver xanthine dehydrogenase. |
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| Journal |
J Biol Chem 242:4097-107 (1967) |
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| Reference |
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| Authors |
Smith ST, Rajagopalan KV, Handler P. |
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| Title |
Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus. |
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| Journal |
J Biol Chem 242:4108-17 (1967) |
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| Reference |
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| Authors |
Ikegami T, Nishino T |
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| Title |
The presence of desulfo xanthine dehydrogenase in purified and crude enzyme preparations from rat liver. |
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| Journal |
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| Reference |
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| Authors |
Engerson TD, McKelvey TG, Rhyne DB, Boggio EB, Snyder SJ, Jones HP |
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| Title |
Conversion of xanthine dehydrogenase to oxidase in ischemic rat tissues. |
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| Journal |
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| Reference |
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| Authors |
Saito T, Nishino T, Tsushima K |
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| Title |
Interconversion between NAD-dependent and O2-dependent types of rat liver xanthine dehydrogenase and difference in kinetic and redox properties between them. |
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| Journal |
Adv Exp Med Biol 253B:179-83 (1989) |
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| Reference |
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| Authors |
Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S. |
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| Title |
Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization. |
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| Journal |
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| Reference |
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| Authors |
Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T. |
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| Title |
Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF. |
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| Title |
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Truglio JJ, Theis K, Leimkuhler S, Rappa R, Rajagopalan KV, Kisker C. |
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| Title |
Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus. |
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| Journal |
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| Reference |
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| Authors |
Hille R. |
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| Title |
The Mononuclear Molybdenum Enzymes. |
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| Journal |
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| Reference |
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| Authors |
Taibi G, Di Gaudio F, Nicotra CM |
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| Title |
Xanthine dehydrogenase processes retinol to retinoic acid in human mammary epithelial cells. |
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| Journal |
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| Reference |
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| Authors |
Nishino T, Okamoto K, Eger BT, Pai EF, Nishino T |
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| Title |
Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase. |
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| Journal |
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| Other DBs |
| ExplorEnz - The Enzyme Database: | 1.17.1.4 |
| ExPASy - ENZYME nomenclature database: | 1.17.1.4 |
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