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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Xanthindehydrogenase</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><table class="wikitable hintergrundfarbe-basis infobox float-right" id="Vorlage_Infobox_Protein_" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">
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<th colspan="3" style="background:#90EE90; color:#202122;">Xanthindehydrogenase
</th></tr>
<tr style="text-align:center;">
<td colspan="3"><span typeof="mw:File"></span>
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<td colspan="3" class="hintergrundfarbe1" style="text-align:center; font-size:smaller; font-weight:bold;">Bändermodell des <u>Monomer</u> der Xanthinoxidase aus Rind, pdb <a rel="nofollow" class="external text" href="http://www.rcsb.org/pdb/explore.do?structureId=1FIQ">1FIQ</a>. Gebundene Cofaktoren, FAD (rot), FeS-cluster (orange), Molybdän-Cofactor mit Molybdän (gelb) und der gebundene Inhibitor Salicylat (blau), sind hervorgehoben.
</td></tr>
<tr>
<td colspan="3" class="hintergrundfarbe1" style="font-size:smaller;">
<p>Vorhandene Strukturdaten: <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/2ckj">2ckj</a></span>, <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/2e1q">2e1q</a></span>
</p>
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<tr>
<th colspan="3" style="background:#90EE90; color:#202122;;">Eigenschaften des menschlichen Proteins
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<tr>
<td><a href="Molare_Masse" title="Molare Masse">Masse</a>/Länge <a href="Prim%C3%A4rstruktur" title="Primärstruktur">Primärstruktur</a>
</td>
<td colspan="2" style="text-align:center;">146 <a href="Dalton_(Einheit)" class="mw-redirect" title="Dalton (Einheit)">kDa</a> / 1332 <a href="Aminos%C3%A4uren" title="Aminosäuren">Aminosäuren</a>
</td></tr>
<tr>
<td><a href="Sekund%C3%A4rstruktur" title="Sekundärstruktur">Sekundär-</a> bis <a href="Quart%C3%A4rstruktur" title="Quartärstruktur">Quartärstruktur</a>
</td>
<td colspan="2" style="text-align:center;">Homodimer
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<td><a href="Koenzym" class="mw-redirect" title="Koenzym">Kofaktor</a>
</td>
<td colspan="2" style="text-align:center;">2 (2Fe-2S), <a href="Flavin-Adenin-Dinukleotid" title="Flavin-Adenin-Dinukleotid">FAD</a>, <a href="Molybdopterin" title="Molybdopterin">Molybdopterin</a>
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<tr>
<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<tr>
<td><a href="Human_Genome_Organisation" title="Human Genome Organisation">Gen-Namen</a>
</td>
<td colspan="2" class="" style="text-align:center;"><i><a rel="nofollow" class="external text" href="https://www.genenames.org/tools/search/#!/all?query=12805">XDH</a></i>, XO, XS, XDHA
</td></tr>
<tr>
<td>Externe IDs
</td>
<td colspan="2" class="">
<ul><li><a href="Online_Mendelian_Inheritance_in_Man" title="Online Mendelian Inheritance in Man">OMIM</a>: <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/omim/607633">607633</a></li>
<li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P47989">P47989</a></li>
<li><a href="Mouse_Genome_Informatics" title="Mouse Genome Informatics">MGI</a>: <a rel="nofollow" class="external text" href="https://www.informatics.jax.org/marker/MGI:98973">98973</a></li>
<li><a href="CAS-Nummer" title="CAS-Nummer">CAS-Nummer</a>: <span title="Untervorlage eingebunden: CASRN"></span><a rel="nofollow" class="external text" href="https://commonchemistry.cas.org/detail?cas_rn=9002-17-9">9002-17-9</a><span class="editoronly" style="display:none;"></span></li></ul>
</td></tr>
<tr>
<th colspan="3" style="background:#90EE90; color:#202122;">Enzymklassifikation
</th></tr>
<tr>
<td><a href="EC-Nummer" title="EC-Nummer">EC, Kategorie</a>
</td>
<td colspan="2" class="" style="text-align:center;"><a rel="nofollow" class="external text" href="https://www.brenda-enzymes.org/enzyme.php?ecno=1.17.3.2">1.17.3.2</a>, <a href="Oxidoreduktase" class="mw-redirect" title="Oxidoreduktase">Oxidoreduktase</a>
</td></tr>
<tr>
<td>Reaktionsart
</td>
<td colspan="2" style="text-align:center;"><a href="Hydroxylierung" title="Hydroxylierung">Hydroxylierung</a>
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<tr>
<td>Substrat
</td>
<td colspan="2" style="text-align:center;">Xanthin + 2 NAD<sup>+</sup> + 2 H<sub>2</sub>O
</td></tr>
<tr>
<td>Produkte
</td>
<td colspan="2" style="text-align:center;">Harnsäure + 2 NADH + 2 H<sup>+</sup>
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<tr>
<th colspan="3" style="background:#90EE90; color:#202122;">Vorkommen
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<td style="background:#C3FDB8; color:#202122;">Homologie-Familie
</td>
<td colspan="2" style="text-align:center;"><a rel="nofollow" class="external text" href="http://hogenom.univ-lyon1.fr/query_sequence?seq=P47989">Xanthindehydrogenase</a>
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<td style="background:#C3FDB8; color:#202122;">Übergeordnetes <a href="Taxon" title="Taxon">Taxon</a>
</td>
<td colspan="2" style="text-align:center;"><a href="Lebewesen" title="Lebewesen">Lebewesen</a>
</td></tr>
<tr>
<td colspan="3" style="background:#90EE90; color:#202122; text-align:center;"><a href="Homologie_(Genetik)#Homologie_zwischen_verdoppelten_oder_fremden_Genen" title="Homologie (Genetik)">Orthologe</a>
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;">
</td>
<td style="background:#C3FDB8; color:#202122; text-align:center;">Mensch
</td>
<td style="background:#C3FDB8; color:#202122; text-align:center;">Hausmaus
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;"><a href="Entrez_Gene" title="Entrez Gene">Entrez</a>
</td>
<td><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=retrieve&dopt=default&list_uids=7498&rn=1">7498</a></span>
</td>
<td><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=retrieve&dopt=default&list_uids=22436&rn=1">22436</a></span>
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;"><a href="Ensembl" title="Ensembl">Ensembl</a>
</td>
<td><span class=""><small><small><a rel="nofollow" class="external text" href="http://www.ensembl.org/Homo_sapiens/geneview?gene=ENSG00000158125;db=core">ENSG00000158125</a></small></small></span>
</td>
<td><span class=""><small><small><a rel="nofollow" class="external text" href="http://www.ensembl.org/Mus_musculus/geneview?gene=ENSMUSG00000024066;db=core">ENSMUSG00000024066</a></small></small></span>
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;"><a href="UniProt" title="UniProt">UniProt</a>
</td>
<td><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P47989">P47989</a>
</td>
<td><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/Q00519">Q00519</a>
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<td style="background:#C3FDB8; color:#202122;"><a href="National_Center_for_Biotechnology_Information" title="National Center for Biotechnology Information">Refseq</a> (mRNA)
</td>
<td><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_000379">NM_000379</a>
</td>
<td><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NM_011723">NM_011723</a>
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;"><a href="National_Center_for_Biotechnology_Information" title="National Center for Biotechnology Information">Refseq</a> (Protein)
</td>
<td><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_000370">NP_000370</a>
</td>
<td><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?val=NP_035853">NP_035853</a>
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;"><a href="Genlocus" title="Genlocus">Genlocus</a>
</td>
<td><span class=""> <a rel="nofollow" class="external text" href="https://genome.ucsc.edu/cgi-bin/hgTracks?org=Human&position=chr2:31334309-31414749">Chr 2: 31.33 – 31.41 Mb</a> </span>
</td>
<td><span class=""> <a rel="nofollow" class="external text" href="https://genome.ucsc.edu/cgi-bin/hgTracks&position=chr17:73883895-73950196">Chr 17: 73.88 – 73.95 Mb</a> </span>
</td></tr>
<tr>
<td style="background:#C3FDB8; color:#202122;"><a href="PubMed" title="PubMed">PubMed</a>-Suche
</td>
<td><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=7498">7498</a></span>
</td>
<td><span class=""><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=22436">22436</a></span>
<p><span class="editoronly" style="display:none;"></span>
</p>
</td></tr></tbody></table><p><span class="editoronly" style="display:none;"></span>
</p><p><b>Xanthindehydrogenase</b> (XDH) und <b>Xanthinoxidase</b> (XO, manchmal auch XAO) sind zwei unterschiedliche Formen desselben <a href="Metalloenzym" class="mw-redirect" title="Metalloenzym">Metalloenzyms</a> (eine <a href="Hydroxylase" class="mw-redirect" title="Hydroxylase">Hydroxylase</a>), welches die zweistufige <a href="Oxidation" title="Oxidation">Oxidation</a> von <a href="Hypoxanthin" title="Hypoxanthin">Hypoxanthin</a> über <a href="Xanthin" title="Xanthin">Xanthin</a> zur <a href="Harns%C3%A4ure" title="Harnsäure">Harnsäure</a> katalysiert. Im Menschen findet es sich hauptsächlich in der Leber, im Dünndarm und in Brustdrüsenzellen<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>. In seiner XDH-Form nutzt es in beiden Reaktionen bevorzugt <a href="NADH" class="mw-redirect" title="NADH">NAD<sup>+</sup></a> als <a href="Elektronenakzeptor" title="Elektronenakzeptor">Elektronenakzeptor</a>.<sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup>
</p><p>Oxidation von Hypoxanthin zu Xanthin durch XDH<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>:
</p><p> + NAD<sup>+</sup> + H<sub>2</sub>O → + NADH + H<sup>+</sup>
</p><p>Oxidation von Xanthin zu Harnsäure durch XDH<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup>:
</p><p> + NAD<sup>+</sup> + H<sub>2</sub>O → + NADH + H<sup>+</sup>
</p><p>Das <i><a href="In_vivo" title="In vivo">in vivo</a></i> ursprünglich als XDH vorliegende Enzym<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> kann leicht in XO umgewandelt werden (z. B. bei einer <a href="Hypoxie" class="mw-disambig" title="Hypoxie">Hypoxie</a>).<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> In dieser Form bevorzugt es molekularen Sauerstoff als Elektronenakzeptor<sup id="cite_ref-8" class="reference"><a href="#cite_note-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup>.
</p><p>Oxidation von Hypoxanthin zu Xanthin durch XO<sup id="cite_ref-9" class="reference"><a href="#cite_note-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup>:
</p><p> + O<sub>2</sub> + H<sub>2</sub>O → + H<sub>2</sub>O<sub>2</sub>
</p><p>Oxidation von Xanthin zu Harnsäure durch XO<sup id="cite_ref-10" class="reference"><a href="#cite_note-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup>:
</p><p> + O<sub>2</sub> + H<sub>2</sub>O → + H<sub>2</sub>O<sub>2</sub>
</p><p>Das Enzym besteht aus zwei identischen Untereinheiten, deren aktive Zentren je ein <a href="Molybd%C3%A4n" title="Molybdän">Molybdänatom</a>, gebunden in Form des Molybdän-Cofaktors (MoCo), aufweisen.<sup id="cite_ref-11" class="reference"><a href="#cite_note-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> Jede Untereinheit enthält zudem zwei unterscheidbare <a href="Eisen-Schwefel-Cluster" title="Eisen-Schwefel-Cluster">Zwei-Eisen-zwei-Schwefel-Cluster</a> (2Fe-2S) und ein <a href="Flavin-Adenin-Dinucleotid" class="mw-redirect" title="Flavin-Adenin-Dinucleotid">FAD</a>-Molekül. In Prokaryoten werden die MoCo-, (2Fe-2S)- und FAD-Domäne von zwei bzw. drei <a href="Gen" title="Gen">Genen</a> kodiert, in Eukaryoten sind die Domänen in einem Gen fusioniert. Das Enzym kommt daher in <a href="Eukaryoten" title="Eukaryoten">Eukaryoten</a> als <a href="Dimer" title="Dimer">Homodimer</a> vor, in <a href="Prokaryoten" title="Prokaryoten">Prokaryoten</a> als Heterotetramer bzw. Heterohexamer.
</p><p>Erhöhter Harnsäurespiegel ist als <a href="Gicht" title="Gicht">Gicht</a> bekannt. Gicht kann daher auch mit einem <a href="Inhibitor" title="Inhibitor">Inhibitor</a> der Xanthinoxidase behandelt werden; zum Beispiel <a href="Allopurinol" title="Allopurinol">Allopurinol</a> oder <a href="Febuxostat" title="Febuxostat">Febuxostat</a>. Allopurinol bindet sich fest an die reduzierte Form der Xanthinoxidase und inaktiviert sie somit. Dadurch wird die Produktion der schwerlöslichen Harnsäure verringert und die Konzentration der besser löslichen Verbindungen <a href="Xanthin" title="Xanthin">Xanthin</a> und <a href="Hypoxanthin" title="Hypoxanthin">Hypoxanthin</a> erhöht.
</p>
<div class="mw-heading mw-heading2"><h2 id="Literatur">Literatur</h2></div>
<ul><li>L. G. Nagler und L. S. Vartanyan: <i>Subunit structure of bovine milk xanthine oxidase. Effect of limited cleavage by proteolytic enzymes on activity and structure.</i> <a href="Biochim_Biophys_Acta" class="mw-redirect" title="Biochim Biophys Acta">Biochim Biophys Acta</a>. 427/1/<b>1976</b>:78-90-<a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1260010?dopt=Abstract">PMID 1260010</a></li>
<li>J. J. Truglio et al.: <i>Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus.</i> Structure. 10/1/<b>2002</b>:115-25. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/11796116?dopt=Abstract">PMID 11796116</a></li>
<li>S. T. Smith et al.: <i>Purification and properties of xanthine dehydroganase from Micrococcus lactilyticus.</i> <a href="J_Biol_Chem" class="mw-redirect" title="J Biol Chem">J Biol Chem</a>. 242/18/<b>1976</b>:4108-4117. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/6061702?dopt=Abstract">PMID 6061702</a></li></ul>
<div class="mw-heading mw-heading2"><h2 id="Weblinks">Weblinks</h2></div>
<div class="sisterproject" style="margin:0.1em 0 0 0;"><div class="noviewer" style="display:inline-block; line-height:10px; min-width:1.6em; text-align:center;" aria-hidden="true" role="presentation"><span class="mw-default-size" typeof="mw:File"><span title="Wikibooks"></span></span></div><b><a href="https://de.wikibooks.org/wiki/Biochemie_und_Pathobiochemie:_Purinabbau" class="extiw external" title="b:Biochemie und Pathobiochemie: Purinabbau">Wikibooks: Biochemie und Pathobiochemie: Purinabbau</a></b> – Lern- und Lehrmaterialien</div>
<div class="sisterproject" style="margin:0.1em 0 0 0;"><div class="noviewer" style="display:inline-block; line-height:10px; min-width:1.6em; text-align:center;" aria-hidden="true" role="presentation"><span class="mw-default-size" typeof="mw:File"><span title="Wikibooks"></span></span></div><b><a href="https://de.wikibooks.org/wiki/Biochemie_und_Pathobiochemie:_Purin-Stoffwechsel" class="extiw external" title="b:Biochemie und Pathobiochemie: Purin-Stoffwechsel">Wikibooks: Biochemie und Pathobiochemie: Purin-Stoffwechsel</a></b> – Lern- und Lehrmaterialien</div>
<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<ol class="references">
<li id="cite_note-1"><span class="mw-cite-backlink"><a href="#cite_ref-1">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://www.proteinatlas.org/ENSG00000158125-XDH"><i>The Human Protein Atlas: XHD</i></a> Eintrag zu Xanthindehydrogenase im <a href="Human_Protein_Atlas" title="Human Protein Atlas">Human Protein Atlas</a>. Abgerufen am 13. März 2024.</span>
</li>
<li id="cite_note-2"><span class="mw-cite-backlink"><a href="#cite_ref-2">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P47989/entry"><i>UniProt: XDH_HUMAN</i></a> Eintrag zu humaner Xanthindehydrogenase/oxidase in <a href="UniProt" title="UniProt">UniProt</a>. Abgerufen am 9. März 2024.</span>
</li>
<li id="cite_note-3"><span class="mw-cite-backlink"><a href="#cite_ref-3">↑</a></span> <span class="reference-text">Usamah S. Kayyali, Cameron Donaldson, Hailu Huang, Raja Abdelnour und Paul M. Hassoun: <cite style="font-style:italic">Phosphorylation of Xanthine Dehydrogenase/Oxidase in Hypoxia</cite>. In: <cite style="font-style:italic"><a href="Journal_of_Biological_Chemistry" title="Journal of Biological Chemistry">Journal of Biological Chemistry</a></cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>276</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>17</span>, 27. April 2001, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>14359–14365</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1074/jbc.M010100200">10.1074/jbc.M010100200</a></span>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Xanthindehydrogenase&rft.atitle=Phosphorylation+of+Xanthine+Dehydrogenase%2FOxidase+in+Hypoxia&rft.au=Usamah+S.+Kayyali%2C+Cameron+Donaldson%2C+Hailu+Huang%2C+...&rft.date=2001-04-27&rft.doi=10.1074%2Fjbc.M010100200&rft.genre=journal&rft.issue=17&rft.jtitle=Journal+of+Biological+Chemistry&rft.pages=14359-14365&rft.volume=276" style="display:none"> </span></span>
</li>
<li id="cite_note-4"><span class="mw-cite-backlink"><a href="#cite_ref-4">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://www.genome.jp/entry/R01768"><i>KEGG: Reaktion R01768</i></a> Eintrag zu Hypoxanthin: NAD+ Oxidoreduktase in <a href="KEGG" class="mw-redirect" title="KEGG">KEGG</a>. Abgerufen am 9. März 2024.</span>
</li>
<li id="cite_note-5"><span class="mw-cite-backlink"><a href="#cite_ref-5">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://www.genome.jp/entry/R02103"><i>KEGG: Reaktion R02103</i></a> Eintrag zu Xanthin: NAD+ Oxidoreduktase in <a href="KEGG" class="mw-redirect" title="KEGG">KEGG</a>. Abgerufen am 9. März 2024.</span>
</li>
<li id="cite_note-6"><span class="mw-cite-backlink"><a href="#cite_ref-6">↑</a></span> <span class="reference-text">Tomoko Nishino, Ken Okamoto, Bryan T. Eger, Emil F. Pai und Takeshi Nishino: <cite style="font-style:italic">Mammalian xanthine oxidoreductase – mechanism of transition from xanthine dehydrogenase to xanthine oxidase</cite>. In: <cite style="font-style:italic"><a href="FEBS_Journal" title="FEBS Journal">FEBS Journal</a></cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>275</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>13</span>, Juli 2008, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>3278–3289</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1111/j.1742-4658.2008.06489.x">10.1111/j.1742-4658.2008.06489.x</a></span>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Xanthindehydrogenase&rft.atitle=Mammalian+xanthine+oxidoreductase+-+mechanism+of+transition+from+xanthine+dehydrogenase+to+xanthine+oxidase&rft.au=Tomoko+Nishino%2C+Ken+Okamoto%2C+Bryan+T.+Eger%2C+...&rft.date=2008-07&rft.doi=10.1111%2Fj.1742-4658.2008.06489.x&rft.genre=journal&rft.issue=13&rft.jtitle=FEBS+Journal&rft.pages=3278-3289&rft.volume=275" style="display:none"> </span></span>
</li>
<li id="cite_note-7"><span class="mw-cite-backlink"><a href="#cite_ref-7">↑</a></span> <span class="reference-text">Jeffrey S. Wiezorek, Douglas H. Brown, David E. Kupperman und Clifford A. Brass: <cite style="font-style:italic">Rapid Conversion to High Xanthine Oxidase Activity in Viable Kupifer Cells
during Hypoxia</cite>. In: <cite style="font-style:italic"><a href="Journal_of_Clinical_Investigation" title="Journal of Clinical Investigation">Journal of Clinical Investigation</a></cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>94</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>6</span>, 1. Dezember 1994, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>2224–2230</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1172/JCI117584">10.1172/JCI117584</a></span>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Xanthindehydrogenase&rft.atitle=Rapid+Conversion+to+High+Xanthine+Oxidase+Activity+in+Viable+Kupifer+Cells%0Aduring+Hypoxia&rft.au=Jeffrey+S.+Wiezorek%2C+Douglas+H.+Brown%2C+David+E.+Kupperman+und+Clifford+A.+Brass&rft.date=1994-12-01&rft.doi=10.1172%2FJCI117584&rft.genre=journal&rft.issue=6&rft.jtitle=Journal+of+Clinical+Investigation&rft.pages=2224-2230&rft.volume=94" style="display:none"> </span></span>
</li>
<li id="cite_note-8"><span class="mw-cite-backlink"><a href="#cite_ref-8">↑</a></span> <span class="reference-text">Usamah S. Kayyali, Cameron Donaldson, Hailu Huang, Raja Abdelnour und Paul M. Hassoun: <cite style="font-style:italic">Phosphorylation of Xanthine Dehydrogenase/Oxidase in Hypoxia</cite>. In: <cite style="font-style:italic"><a href="Journal_of_Biological_Chemistry" title="Journal of Biological Chemistry">Journal of Biological Chemistry</a></cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>276</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>17</span>, 27. April 2001, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>14359–14365</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1074/jbc.M010100200">10.1074/jbc.M010100200</a></span>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Xanthindehydrogenase&rft.atitle=Phosphorylation+of+Xanthine+Dehydrogenase%2FOxidase+in+Hypoxia&rft.au=Usamah+S.+Kayyali%2C+Cameron+Donaldson%2C+Hailu+Huang%2C+...&rft.date=2001-04-27&rft.doi=10.1074%2Fjbc.M010100200&rft.genre=journal&rft.issue=17&rft.jtitle=Journal+of+Biological+Chemistry&rft.pages=14359-14365&rft.volume=276" style="display:none"> </span></span>
</li>
<li id="cite_note-9"><span class="mw-cite-backlink"><a href="#cite_ref-9">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://www.genome.jp/entry/R01769"><i>KEGG: Reaktion R01769</i></a> Eintrag zu Hypoxanthin: Oxygen Oxidoreduktase in <a href="KEGG" class="mw-redirect" title="KEGG">KEGG</a>. Abgerufen am 9. März 2024.</span>
</li>
<li id="cite_note-10"><span class="mw-cite-backlink"><a href="#cite_ref-10">↑</a></span> <span class="reference-text"><a rel="nofollow" class="external text" href="https://www.genome.jp/entry/R02107"><i>KEGG: Reaktion R02107</i></a> Eintrag zu Xanthin: Oxygen Oxidoreduktase in <a href="KEGG" class="mw-redirect" title="KEGG">KEGG</a>. Abgerufen am 9. März 2024.</span>
</li>
<li id="cite_note-11"><span class="mw-cite-backlink"><a href="#cite_ref-11">↑</a></span> <span class="reference-text">Russ Hille, Takeshi Nishino: <cite style="font-style:italic">Xanthine oxidase and xanthine dehydrogenase</cite>. In: <cite style="font-style:italic"><a href="The_FASEB_Journal" title="The FASEB Journal">The FASEB Journal</a></cite>. <span style="white-space:nowrap">Band<span style="display:inline-block;width:.2em"> </span>9</span>, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>11</span>, August 1995, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>995–1003</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1096/fasebj.9.11.7649415">10.1096/fasebj.9.11.7649415</a></span>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Xanthindehydrogenase&rft.atitle=Xanthine+oxidase+and+xanthine+dehydrogenase&rft.au=Russ+Hille%2C+Takeshi+Nishino&rft.date=1995-08&rft.doi=10.1096%2Ffasebj.9.11.7649415&rft.genre=journal&rft.issue=11&rft.jtitle=The+FASEB+Journal&rft.pages=995-1003&rft.volume=9" style="display:none"> </span></span>
</li>
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