Glycogen phosphorylase concentration, as the liver acts as a glucose exporter. In essence, liver phosphorylase is responsive to glucose, which causes a very responsive transition from the R to T form, inactivating it; furthermore, liver phosphorylase is insensitive to AMP. Glycogen phosphorylase was the first allosteric enzyme to be discovered. This accomplishment was one of many landmark achievements made by Carl and Gerty Cori. In 1943, with the help of Arda Green, the pair illustrated that glycogen phosphorylase existed in either the or b forms depending on its phosphorylation state, as well as in the R or T states based on the
Glycogen phosphorylase through greater organization and intersubunit interactions. This rotation of the tower helices leads to a rotation of the two subunits by 10˚ relative to one another, and more importantly disorders residues 282-286 (the 280s loop) that block access to the catalytic site in the T state but do not in the R state. The final, perhaps most curious site on the glycogen phosphorylase protein is the so-called glycogen storage site. Residues 397-437 form this structure, which allows the protein to covalently bind to the glycogen chain a full 30 Å from the catalytic site . This site is most likely