2e1q

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[[Image:2e1q.png|left|200px]]
 
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{{STRUCTURE_2e1q| PDB=2e1q | SCENE= }}
{{STRUCTURE_2e1q| PDB=2e1q | SCENE= }}
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===Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val===
===Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val===
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{{ABSTRACT_PUBMED_17301077}}
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{{ABSTRACT_PUBMED_17301077}}
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==Disease==
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[[http://www.uniprot.org/uniprot/XDH_HUMAN XDH_HUMAN]] Defects in XDH are the cause of xanthinuria type 1 (XU1) [MIM:[http://omim.org/entry/278300 278300]]. Xanthinuria is characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. XU1 is due to isolated xanthine dehydrogenase. XU1 patients can metabolize allopurinol.<ref>PMID:9153281</ref><ref>PMID:10844591</ref><ref>PMID:11379872</ref><ref>PMID:14551354</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/XDH_HUMAN XDH_HUMAN]] Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).<ref>PMID:17301077</ref>
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:017301077</ref><references group="xtra"/>
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<ref group="xtra">PMID:017301077</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ichida, K.]]
[[Category: Ichida, K.]]

Revision as of 19:28, 24 March 2013

Template:STRUCTURE 2e1q

Contents

Crystal Structure of Human Xanthine Oxidoreductase mutant, Glu803Val

Template:ABSTRACT PUBMED 17301077

Disease

[XDH_HUMAN] Defects in XDH are the cause of xanthinuria type 1 (XU1) [MIM:278300]. Xanthinuria is characterized by excretion of very large amounts of xanthine in the urine and a tendency to form xanthine stones. Uric acid is strikingly diminished in serum and urine. XU1 is due to isolated xanthine dehydrogenase. XU1 patients can metabolize allopurinol.[1][2][3][4]

Function

[XDH_HUMAN] Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).[5]

About this Structure

2e1q is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • 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. 2007 Apr;141(4):513-24. Epub 2007 Feb 14. PMID:17301077 doi:10.1093/jb/mvm053
  1. ↑ Ichida K, Amaya Y, Kamatani N, Nishino T, Hosoya T, Sakai O. Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. J Clin Invest. 1997 May 15;99(10):2391-7. PMID:9153281 doi:10.1172/JCI119421
  2. ↑ Levartovsky D, Lagziel A, Sperling O, Liberman U, Yaron M, Hosoya T, Ichida K, Peretz H. XDH gene mutation is the underlying cause of classical xanthinuria: a second report. Kidney Int. 2000 Jun;57(6):2215-20. PMID:10844591 doi:10.1046/j.1523-1755.2000.00082.x
  3. ↑ Sakamoto N, Yamamoto T, Moriwaki Y, Teranishi T, Toyoda M, Onishi Y, Kuroda S, Sakaguchi K, Fujisawa T, Maeda M, Hada T. Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria. Hum Genet. 2001 Apr;108(4):279-83. PMID:11379872
  4. ↑ Gok F, Ichida K, Topaloglu R. Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria. Nephrol Dial Transplant. 2003 Nov;18(11):2278-83. PMID:14551354
  5. ↑ 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. 2007 Apr;141(4):513-24. Epub 2007 Feb 14. PMID:17301077 doi:10.1093/jb/mvm053

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