Xanthine dehydrogenase Information & Xanthine dehydrogenase Links at HealthHaven.com

xanthine dehydrogenase
Identifiers
EC number	1.17.1.4
CAS number	9054-84-6
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB	structures
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles

Xanthine dehydrogenase
	; PDB rendering based on 1fiq.
Available structures
	1fiq, 1wyg, 2ckj, 2e1q, 2e3t
Identifiers
Symbols	XDH; XO; XOR
External IDs	OMIM: 607633 MGI: 98973 HomoloGene: 324 GeneCards: XDH Gene
EC number	1.17.1.4
Gene ontology
Molecular function	• xanthine dehydrogenase activity; • xanthine oxidase activity; • iron ion binding; • electron carrier activity; • molybdenum ion binding; • metal ion binding; • 2 iron, 2 sulfur cluster binding;
Cellular component	• peroxisome;
Biological process	• electron transport; • lactation; • regulation of epithelial cell differentiation;
RNA expression pattern
	More reference expression data
Orthologs

edit

Xanthine dehydrogenase, also known as XDH, is a protein that, in humans, is encoded by the XDH gene.^[1]^[2]

[edit] Function

Xanthine dehydrogenase belongs to the group of molybdenum-containing hydroxylases involved in the oxidative metabolism of purines. The enzyme is a homodimer. Xanthine dehydrogenase can be converted to xanthine oxidase by reversible sulfhydryl oxidation or by irreversible proteolytic modification.^[1]

Xanthine dehydrogenase catalyzes the following chemical reaction:

xanthine + NAD⁺ + H₂O $\rightleftharpoons$ urate + NADH + H⁺

The three substrates of this enzyme are xanthine, NAD⁺, and H₂O, whereas its three products are urate, NADH, and H⁺.

This enzyme belongs to the family of oxidoreductases, to be specific, those acting on CH or CH2 group with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is xanthine:NAD+ oxidoreductase. Other names in common use include NAD+-xanthine dehydrogenase, xanthine-NAD+ oxidoreductase, xanthine/NAD+ oxidoreductase, and xanthine oxidoreductase. This enzyme participates in purine metabolism.

[edit] Clinical significance

Defects in xanthine dehydrogenase cause xanthinuria, may contribute to adult respiratory stress syndrome, and may potentiate influenza infection through an oxygen metabolite-dependent mechanism.^[1]

[edit] See also

xanthine oxidase

[edit] References

^ ^a ^b ^c "Entrez Gene: XDH xanthine dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7498.
^ Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T (November 1993). "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene 133 (2): 279–84. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.

[edit] Further reading

Battelli MG, Lorenzoni E (1982). "Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver". Biochem. J. 207: 133–8. PMID 6960894.
Corte ED, 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: 739–45. PMID 4342395.
PARZEN SD, FOX AS (1964). "PURIFICATION OF XANTHINE DEHYDROGENASE FROM DROSOPHILA MELANOGASTER". Biochim. Biophys. Acta. 92: 465–71. PMID 14264879.
Rajagopalan KV, Handler P (1967). "Purification and properties of chicken liver xanthine dehydrogenase". J. Biol. Chem. 242: 4097–107. PMID 4294045.
Smith ST, Rajagopalan KV, Handler P (1967). "Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus". J. Biol. Chem. 242: 4108–17. PMID 6061702.
Parschat K, Canne C, Huttermann J, Kappl R, Fetzner S (2001). "Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization". Biochim. Biophys. Acta. 1544: 151–65. PMID 11341925.
N, Nishino T (1993). "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene. 133: 279–84. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.
Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (2000). "Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion". Proc. Natl. Acad. Sci. U. S. A. 97: 10723–8. doi:10.1073/pnas.97.20.10723. PMID 11005854.
C (Camb). "Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus". S Structure.: 115–25. PMID 11796116.
Hille R (1996). "The Mononuclear Molybdenum Enzymes". Chem. Rev. 96: 2757–2816. doi:10.1021/cr950061t. PMID 11848841.

Meneshian A, Bulkley GB (2002). "The physiology of endothelial xanthine oxidase: from urate catabolism to reperfusion injury to inflammatory signal transduction.". Microcirculation (New York, N.Y. : 1994) 9 (3): 161–75. doi:10.1038/sj.mn.7800136. PMID 12080414.
Xu P, Huecksteadt TP, Harrison R, Hoidal JR (1995). "Molecular cloning, tissue expression of human xanthine dehydrogenase.". Biochem. Biophys. Res. Commun. 215 (1): 429. doi:10.1006/bbrc.1995.2482. PMID 7575623.
Xu P, Zhu XL, Huecksteadt TP, et al. (1995). "Assignment of human xanthine dehydrogenase gene to chromosome 2p22.". Genomics 23 (1): 289–91. doi:10.1006/geno.1994.1498. PMID 7829092.
Minoshima S, Wang Y, Ichida K, et al. (1994). "Mapping of the gene for human xanthine dehydrogenase (oxidase) (XDH) to band p23 of chromosome 2.". Cytogenet. Cell Genet. 68 (1-2): 52–3. doi:10.1159/000133887. PMID 7956358.
Rytkönen EM, Halila R, Laan M, et al. (1994). "The human gene for xanthine dehydrogenase (XDH) is localized on chromosome band 2q22.". Cytogenet. Cell Genet. 68 (1-2): 61–3. doi:10.1159/000133890. PMID 7956361.
Xu P, Huecksteadt TP, Harrison R, Hoidal JR (1994). "Molecular cloning, tissue expression of human xanthine dehydrogenase.". Biochem. Biophys. Res. Commun. 199 (2): 998–1004. doi:10.1006/bbrc.1994.1328. PMID 8135849.
Ichida K, Amaya Y, Noda K, et al. (1993). "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene.". Gene 133 (2): 279–84. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.
Satoh A, Sasago S, Takahashi S, Kato N (1993). "Regulation of xanthine dehydrogenase in rat liver in response to peroxisome proliferators.". Biochem. Biophys. Res. Commun. 195 (2): 751–7. doi:10.1006/bbrc.1993.2109. PMID 8373410.
Xu P, Huecksteadt TP, Hoidal JR (1997). "Molecular cloning and characterization of the human xanthine dehydrogenase gene (XDH).". Genomics 34 (2): 173–80. doi:10.1006/geno.1996.0262. PMID 8661045.
Saksela M, Raivio KO (1996). "Cloning and expression in vitro of human xanthine dehydrogenase/oxidase.". Biochem. J. 315 ( Pt 1): 235–9. PMID 8670112.
Many A, Westerhausen-Larson A, Kanbour-Shakir A, Roberts JM (1996). "Xanthine oxidase/dehydrogenase is present in human placenta.". Placenta 17 (5-6): 361–5. doi:10.1016/S0143-4004(96)90061-2. PMID 8829220.
Hellsten Y, Frandsen U, Orthenblad N, et al. (1997). "Xanthine oxidase in human skeletal muscle following eccentric exercise: a role in inflammation.". J. Physiol. (Lond.) 498 ( Pt 1): 239–48. PMID 9023782.
Ichida K, Amaya Y, Kamatani N, et al. (1997). "Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria.". J. Clin. Invest. 99 (10): 2391–7. doi:10.1172/JCI119421. PMID 9153281.
Rouquette M, Stevens C, Blake DR, et al. (1998). "Expression of xanthine oxidase activity in human endothelial cells as a function of cell density.". Biochem. Soc. Trans. 25 (3): 532S. PMID 9388748.
Newaz MA, Adeeb NN (2000). "Detection of xanthine oxidase in human plasma.". Med. J. Malaysia 53 (1): 70–5. PMID 10968141.
Martelin E, Palvimo JJ, Lapatto R, Raivio KO (2000). "Nuclear factor Y activates the human xanthine oxidoreductase gene promoter.". FEBS Lett. 480 (2-3): 84–8. doi:10.1016/S0014-5793(00)01909-8. PMID 11034305.
Stiborová M, Frei E, Sopko B, et al. (2002). "Carcinogenic aristolochic acids upon activation by DT-diaphorase form adducts found in DNA of patients with Chinese herbs nephropathy.". Carcinogenesis 23 (4): 617–25. doi:10.1093/carcin/23.4.617. PMID 11960915.
Frederiks WM, Vreeling-Sindelárová H (2002). "Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells.". Acta Histochem. 104 (1): 29–37. doi:10.1078/0065-1281-00629. PMID 11993848.
Cejková J, Ardan T, Filipec M, Midelfart A (2003). "Xanthine oxidoreductase and xanthine oxidase in human cornea.". Histol. Histopathol. 17 (3): 755–60. PMID 12168784.

This EC 1.17 enzyme-related article is a stub. You can help Wikipedia by expanding it.

[entrez-0] "Entrez Gene: XDH xanthine dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7498.

[pmid8224915-1] Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T (November 1993). "Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene". Gene 133 (2): 279–84. doi:10.1016/0378-1119(93)90652-J. PMID 8224915.

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[2]

Contents

[edit] Function

[edit] Clinical significance

[edit] See also

[edit] References

[edit] Further reading