Glycogen phosphorylase longer cause the phosphorylation cascade that ends with formation of (active) glycogen phosphorylase a. These modifications initiated by insulin end glycogenolysis in order to preserve what glycogen stores are left in the cell and trigger glycogenesis (rebuilding of glycogen). Phosphorylase a and phosphorylase b each exist in two forms a T (tense) inactive state and R (relaxed) state. Phosphorylase b is normally in the T state, inactive due to the physiological presence of ATP and Glucose 6 phosphate, and Phosphorylase a is normally in the R state (active). An isoenzyme of glycogen phosphorylase exists in the liver sensitive to glucose
Glycogen-branching enzyme deficiency caused by an autosomal recessive mutation to the GBE1 gene, which leads glycogen branching enzyme activity that is reduced to absent. Subsequently, glycogen molecules are produced with few branches, which greatly decreasing the number of nonreducing ends, drastically slowing the rate at which the molecule can be synthesized or broken down. This causes low levels of muscle glycogen that is very resistant to amylase. Lacking proper glycogen storage, the horse's brain, heart muscle, and skeletal muscles cannot function, leading to rapid death. Most foals with glycogen-branching enzyme deficiency (GBED) are aborted (usually in the second trimester), or are stillborn, and