Phosphorylase Information & Phosphorylase Links at HealthHaven.com

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]

[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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[0] Lehninger Principles of Biochemistry 5th ed. pg. 603

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