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    <!-- http://purl.obolibrary.org/obo/RO_0002233 -->

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    <!-- http://purl.obolibrary.org/obo/CHEBI_16077 -->

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    <!-- http://purl.obolibrary.org/obo/CHEBI_18367 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0019071 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0019071">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">glycogen-glycogenin-2 + n orthophosphate =&gt; limit dextrin-glycogenin-2 + n D-glucose 1-phosphate [PYGL]</rdfs:label>
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        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed10949035</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed2667896</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 4371590</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome, http://www.reactome.org</ns3:IAO_0000119>
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        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The phosphorylated PYGL dimer (a form) of glycogen phosphorylase catalyzes the reaction of orthophosphate and glycogen-glycogenin 1 to form D-glucose 1-phosphate and limit dextrin-glycogenin 1. This reaction occurs on the surfaces of cytosolic glycogen granules. Non-phosphorylated PYGL dimers (b form) are catalytically inactive even in the presence of AMP. In the body, this reaction takes place in the liver where its dependence on hormonally stimulated PYGL phosphorylation (and lack of sensitivity to AMP) allow glucose mobilization in response to a demand for glucose from the rest of the body (Newgard et al. 1989; Rath et al. 2000).</rdfs:comment>
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    <!-- http://purl.obolibrary.org/obo/HINO_0024188 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0024225 -->

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    <!-- http://purl.obolibrary.org/obo/INO_0000040 -->

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