Figure 1From: Quantification of the glycogen cascade system: the ultrasensitive responses of liver glycogen synthase and muscle phosphorylase are due to distinctive regulatory designsEnzyme cascades involved in the regulation of glycogen synthesis and degradation in (A) Skeletal Muscle (B) Liver. Nomenclature: Active enzyme form is indicated by an affix 'a' and the corresponding inactive form is indicated by an affix 'b'. R2C2, cyclic AMP dependent protein kinase (CAPK); C, catalytic subunit of CAPK; PP1, phosphatase-1; PrP2, phosphatases-2A; PK, Phosphorylase kinase; GP, glycogen phosphorylase; GS, Glycogen synthase; Glu6P, glucose-6-phosphate; PP1 Inhibitor-1, Inhibitor of PP1; Km1 to Km8 are Michaelis-Menten constants, k1 to k8 are rate constants, K11, K22, Kd are dissociation constants as shown in the figure. Positive and negative signs indicate the activation and inhibition of a reaction respectively. In the muscle (Fig. 1A), cAMP activated CAPK catalyzes the phosphorylation of GS, PK and inhibitor-1. Phosphorylated PK activates GP-b. Active phosphatase-2A is assumed to inactivate inhibitor-1, whereas PP1 catalyzes the dephosphorylation of GS, GP and PK. In liver (Fig. 1B), GP-a catalyzes the allosteric inactivation of GS phosphatase and inhibitor-1 does not appear to be involved in the regulation of PP1.Back to article page