Phosphorylase
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Phosphorylase is a family of allosteric enzymes that catalyze the production of glucose-1-phosphate from a polyglucose such as glycogen, starch or maltodextrin.
More generally, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor. Do not confuse this enzyme with a phosphatase or a kinase. A phosphatase removes a phosphate group from a donor, while a kinase transfers a phosphate group from a donor (usually ATP) to an acceptor.
The phosphorylases are named by prepending the name of the substrate, e.g. glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase.
All known phosphorylases share catalytic and structural properties [1].
Phosphorylase a is the active form of glycogen phosphorylase that is derived from the phosphorylation of the inactive form, phosphorylase b .
[edit] See also
[edit] External links
Hexosyltransferases: Glucosyltransferases (Glycogen branching enzyme, Glycogen synthase, Glycogen phosphorylase, Phosphorylase/Myophosphorylase) - Glucuronosyltransferase
Pentosyltransferases: Adenine phosphoribosyltransferase - Hypoxanthine-guanine phosphoribosyltransferase - ADP Ribose (Cholera toxin, Diphtheria toxin, Pertussis toxin, Poly ADP ribose polymerase)