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 debranching enzyme a glycogen branch down to four glucose residues, it will not remove further residues. Glycogen debranching enzymes assist phosphorylase, the primary enzyme involved in glycogen breakdown, mobilize glycogen stores. Phosphorylase can only cleave α-1,4- glycosidic bond between adjacent glucose molecules in glycogen but branches exist as α-1,6 linkages. When phosphorylase reaches four residues from a branching point it stops cleaving; because 1 in 10 residues is branched, cleavage by phosphorylase alone would not be sufficient in mobilizing glycogen stores. Before phosphorylase can resume catabolism, debranching enzymes perform two functions: Thus the debranching enzymes, transferase and α-1,6- glucosidase converts the branched