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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Polyphenoloxidase</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_Phenolase_der_Süßkartoffel_(Ipomoea_batatas)" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">
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<th colspan="3" style="background:#90EE90; color:#202122;">Phenolase der <a href="S%C3%BC%C3%9Fkartoffel" title="Süßkartoffel">Süßkartoffel</a> (<i>Ipomoea batatas</i>)
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<p>Vorhandene Strukturdaten: <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1bt1">1bt1</a></span>, <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1bt2">1bt2</a></span>, <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1bt3">1bt3</a></span>, <span class=""><a rel="nofollow" class="external text" href="https://www.rcsb.org/structure/1bug">1bug</a></span>
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<td><a href="Molare_Masse" title="Molare Masse">Masse</a>/Länge <a href="Prim%C3%A4rstruktur" title="Primärstruktur">Primärstruktur</a>
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<td colspan="2" style="text-align:center;">496 Aminosäuren
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<td><a href="Sekund%C3%A4rstruktur" title="Sekundärstruktur">Sekundär-</a> bis <a href="Quart%C3%A4rstruktur" title="Quartärstruktur">Quartärstruktur</a>
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<td colspan="2" style="text-align:center;">Monomer
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<td><a href="Koenzym" class="mw-redirect" title="Koenzym">Kofaktor</a>
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<td colspan="2" style="text-align:center;">2 Kupfer
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<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<td>Externe IDs
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<ul><li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/Q9ZP19">Q9ZP19</a></li></ul>
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<th colspan="3" style="background:#90EE90; color:#202122;">Enzymklassifikation
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<td><a href="EC-Nummer" title="EC-Nummer">EC, Kategorie</a>
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<td colspan="2" class="" style="text-align:center;"><a rel="nofollow" class="external text" href="https://www.brenda-enzymes.org/enzyme.php?ecno=1.10.3.1">1.10.3.1</a>, <a href="Oxidoreduktase" class="mw-redirect" title="Oxidoreduktase">Oxidoreduktase</a>
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<td>Reaktionsart
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<td colspan="2" style="text-align:center;">Oxidation
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<td>Substrat
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<td colspan="2" style="text-align:center;">2 Mono/Diphenol + O<sub>2</sub>
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<td>Produkte
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<td colspan="2" style="text-align:center;">2 o-Dichinon + 2 H<sub>2</sub>O
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<th colspan="3" style="background:#90EE90; color:#202122;">Vorkommen
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<td style="background:#C3FDB8; color:#202122;">Übergeordnetes <a href="Taxon" title="Taxon">Taxon</a>
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<td colspan="2" style="text-align:center;">Pflanzen
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</p><p><b>Phenolase</b>, genauer <b><a href="Chloroplast" title="Chloroplast">chloroplastische</a> Polyphenoloxidase (PPO)</b>, auch <i>Catecholoxidase I</i>, heißt das <a href="Homologie_(Biologie)" title="Homologie (Biologie)">Homolog</a> der <a href="Tyrosinase" title="Tyrosinase">Tyrosinase</a> in Pflanzen. Zusätzlich zu den Reaktionen der Tyrosinase ist sie in der Lage, <a href="Phenole" title="Phenole">Phenole</a> und Catechole zu <a href="Oxidation" title="Oxidation">oxidieren</a>. Diese Reaktionen sorgen für die <a href="Enzymatische_Br%C3%A4unung" title="Enzymatische Bräunung">Bräunung</a> von Pflanzenmaterial nach Verletzung und Kontakt mit Luftsauerstoff. Die entstehenden <a href="Chinone" title="Chinone">Chinone</a> sind giftig für pathogene Mikroorganismen.<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>
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<div class="mw-heading mw-heading2"><h2 id="Enzymatische_Katalyse">Enzymatische Katalyse</h2></div>
<p>Bei der Oxidation von <a href="Brenzcatechin" title="Brenzcatechin">Brenzcatechin</a> in Anwesenheit von Phenolase als Katalysator wird das Dihydroxybenzol in <a href="Benzochinon" class="mw-disambig" title="Benzochinon">Benzochinon</a> umgewandelt:
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<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
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<li id="cite_note-1"><span class="mw-cite-backlink"><a href="#cite_ref-1">↑</a></span> <span class="reference-text">Mayer AM: <cite style="font-style:italic">Polyphenol oxidases in plants and fungi: going places? A review</cite>. In: <cite style="font-style:italic"><a href="Phytochemistry" title="Phytochemistry">Phytochemistry</a></cite>. 67. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>21</span>, November 2006, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>2318–2331</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/10.1016/j.phytochem.2006.08.006">10.1016/j.phytochem.2006.08.006</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16973188?dopt=Abstract">PMID 16973188</a>.<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:Polyphenoloxidase&rft.atitle=Polyphenol+oxidases+in+plants+and+fungi%3A+going+places%3F+A+review&rft.au=Mayer+AM&rft.date=2006-11&rft.doi=10.1016%2Fj.phytochem.2006.08.006&rft.genre=journal&rft.issue=21&rft.jtitle=Phytochemistry&rft.pages=2318-2331&rft.pmid=16973188&rft.volume=67.+Jahrgang" style="display:none"> </span></span>
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