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Figure 1 | Theoretical Biology and Medical Modelling

Figure 1

From: Quantification of the glycogen cascade system: the ultrasensitive responses of liver glycogen synthase and muscle phosphorylase are due to distinctive regulatory designs

Figure 1

Enzyme 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.

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