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| Phosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 The crystal structure of the rabbit muscle glycogen phosphorylase-AMP complex. AMP allosteric site (yellow), phosphorylated Ser14 (orange), glycogen binding site (blue), catalytic site (red).[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 2.4.1.1 | ||||||||
| CAS no. | 9035-74-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Glycogen phosphorylase is one of the phosphorylase enzymes (EC 2.4.1.1). Glycogen phosphorylase catalyzes the rate-limiting step in glycogenolysis in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. Glycogen phosphorylase is also studied as a model protein regulated by both reversible phosphorylation and allosteric effects.