phosphorylases
Not to be confused with phosphatases or protein kinases, phosphorylases are allosteric enzymes that catalyze the transfer of phosphate groups from an inorganic phosphate to an acceptor.
Phosporylases are classified according to the acceptor molecule, and all phosphorylases share catalytic and structural properties. For example, glycogen phosphorylase attacks 1,4 glycosidic linkages in linear glycogens to generate glucose-1-phosphate, which is subsequently converted, by phosphoglucomutase (rev. isomutase) , into glucose-6-phosphate for glycolysis or the pentose-phosphate pathway. Debranching enzymes are required to attack 1,6 glycosidic branching points.
Phosporylases are classified according to the acceptor molecule, and all phosphorylases share catalytic and structural properties. For example, glycogen phosphorylase attacks 1,4 glycosidic linkages in linear glycogens to generate glucose-1-phosphate, which is subsequently converted, by phosphoglucomutase (rev. isomutase) , into glucose-6-phosphate for glycolysis or the pentose-phosphate pathway. Debranching enzymes are required to attack 1,6 glycosidic branching points.