Linked Life Data

48887BiochemicalReaction3992

Source:http://www.reactome.org/biopax/48887BiochemicalReaction3992

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Glycogen synthase catalyzes the addition of glucose residues to the non-reducing end of a (1,4)-alpha-D-glucose multimer formed on glycogenin-1 or -2. (Here the addition of four glucose residues is annotated.) The enzyme is associated with glycogen granules in the cytosol.<p>Glycogen synthase proteins are encoded by two human genes, GYS1 and GYS2. GYS1 protein is abundant in skeletal muscle while GYS2 is abundant in liver. The cytosolic location and glycogen synthase activity of GYS1 protein has been demonstrated in studies of wild-type and mutant proteins expressed in cultured cells in vitro (Cid et al. 2000). Defects in GYS1 protein in vivo are associated with deficient muscle glycogen synthesis and exercise intolerance in vivo (Kollberg et al. 2007). The enzymatic activity of purified GYS2 protein has been characterized experimentally (Westphal and Nuttall 1992). Defects in GYS2 protein in vivo are associated with fasting hypoglycemia and defective glycogen synthesis in the liver (Orho et al. 1998).<p>Human GYS enzymes are inferred to be active as homotetramers, from detailed characterization of the homologous rabbit muscle enzyme (Soderling et al. 1970).<p>GYS activity is regulated by phosphorylation. In its non-phosphorylated â??Iâ?? form, annotated here, the enzyme is active with no added cofactor.<br>
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8 UDP-glucose + ((1,4)-alpha-D-glucosyl}4 glycogenin => 8 UDP + ((1,4)-alpha-D-glucosyl)8 glycogenin [GYS I form]
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2.4.1.11
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