词条 | Phosphorylase | ||||||||||||||||||||
释义 |
| Name = Phosphorylase | EC_number = 2.4.1.1 | CAS_number = 9035-74-9 | IUBMB_EC_number = 2/4/1/1 | GO_code = | image = 1z8d.jpg | width = 270 | caption = }} Phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor. A-B + P {{eqm}} A + P-B They include allosteric enzymes that catalyze the production of glucose-1-phosphate from a glucan 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 1930s discovered the first phosphorylase.[1] FunctionPhosphorylases should not be confused with phosphatases, which remove phosphate groups. In more general terms, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate + hydrogen) to an acceptor, not to be confused with a phosphatase (a hydrolase) or a kinase (a phosphotransferase). A phosphatase removes a phosphate group from a donor using water, whereas a kinase transfers a phosphate group from a donor (usually ATP) to an acceptor.
TypesThe phosphorylases fall into the following categories:
All known phosphorylases share catalytic and structural properties . ActivationPhosphorylase a is the more active R form of glycogen phosphorylase that is derived from the phosphorylation of the less active R form, phosphorylase b with associated AMP. The inactive T form is either phosphorylated by phosphoylase kinase and inhibited by glucose, or dephosphorylated by phosphoprotein phosphatase with inhibition by ATP and/or glucose 6-phosphate. Phosphorylation requires ATP but dephosphorylation releases free inorganic phosphate ions. PathologySome disorders are related to phosphorylases:
See also
References1. ^Lehninger Principles of Biochemistry 5th ed. pg. 603 External links
2 : Transferases|EC 2.4.1 |
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