Phosphorylase
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{{Expert-verify|date=February 2007}}
'''Phosphorylase''' is a family of [[Allosteric regulation|allosteric]] [[enzyme]]s that [[catalysis|catalyze]] the production of [[glucose-1-phosphate]] from a polyglucose such as [[glycogen]], [[starch]] or [[maltodextrin]].
==Function==
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.
==Types==
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 [http://www.expasy.org/cgi-bin/nicedoc.pl?PDOC00095].
==Activation==
'''Phosphorylase a''' is the active form of glycogen phosphorylase that is derived from the phosphorylation of the inactive form, '''phosphorylase b'''.
==Pathology==
Some disorders are related to phosphorylases:
* [[Glycogen storage disease type V]] - muscle glycogen
* [[Glycogen storage disease type VI]] - liver glycogen
==External links==
* {{MeshName|Phosphorylases}}
{{transferase-stub}}
{{Glycosyltransferases}}
[[Category:Transferases]]
[[Category:EC 2.4.1]]
[[ms:Fosforilase]]