Phosphorylase
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Phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.
Phosphorylase is a family of allosteric enzymes that catalyze the production of glucose-1-phosphate from a polyglucose such as glycogen, starch or maltodextrin. Phosphorylase is also a common name used for glycogen phosphorylase in honor of Earl W. Sutherland Jr. who in the late 1930's discovered the first phosphorylase. [1]
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[edit] 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.
[edit] 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 [1].
[edit] Activation
Phosphorylase a is the active form of glycogen phosphorylase that is derived from the phosphorylation of the inactive form, phosphorylase b.
[edit] Pathology
Some disorders are related to phosphorylases:
- Glycogen storage disease type V - muscle glycogen
- Glycogen storage disease type VI - liver glycogen
[edit] References
- ^ Lehninger Principles of Biochemistry 5th ed. pg. 603
[edit] External links
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