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    <!-- http://purl.obolibrary.org/obo/HINO_0001265 -->

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        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PathwayStep1957</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/HINO_0001267 -->

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        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PathwayStep1959</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/HINO_0001268 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0004075 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0004087 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0004090 -->

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        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Arachidonic acid is hydroxylated to 19-HETE by CYP(2)</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/HINO_0014602 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0014602">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE)</rdfs:label>
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        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: Williams, MG, 2012-02-24</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: Williams, MG, 2012-02-24</rdfs:comment>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">GENE ONTOLOGYGO:0097267</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">ISBN978-0-444-53219-0</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed10681399</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed19244215</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 432142816</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome, http://www.reactome.org</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">ReactomeREACT_150134</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Rush, MG, 2012-11-10</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Similar to the lipoxygenases, cytochrome P450 (CYP) enzymes catalyse the hydroxylation and epoxygenation of arachidonic acid.  However, whereas lipoxygenases use an active non-heme iron to abstract hydrogen directly from arachidonic acid, CYPs contain a heme-iron active site that oxidizes its substrate by a different mechanism.  They hydroxylate arachidonic acid between C-5 and C-15 to produce lipoxygenase-like hydroxyeicosatetraenoic acids (HETEs) and add a hydroxyl moiety to the sp3-hybridized omega-carbons to form a unique class of HETEs.  The transfer of oxygen to the unstable arachidonic acid intermediate terminates the reaction by forming HETE or epoxy-eicosatrienoic acid (EETs), respectively (Capdevila et al. 2000, Buczynski et al. 2009, Vance &amp; Vance 2008).</rdfs:comment>
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    <!-- http://purl.obolibrary.org/obo/INO_0000021 -->

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