EC Number   |
General Information |
Reference |
|---|
    2.4.1.1 | evolution |
plants contain two major Pho forms: the plastidial Pho1 or PhoL (low glycogen affinity) encoded by the PHO1 gene and a cytosolic Pho2 or PhoH (high glycogen affinity) encoded by the PHO2 gene |
718691 |
| 2.4.1.1 | malfunction |
mutations that impair glycogen phosphorylase activity leads to McArdle's disease which is characterized by exercise intolerance, muscle fatigue, and cramps. The irreversible inhibition of the enzyme might represent one of the mechanisms that contribute to mercury-dependent muscle toxicity |
-, 736105 |
| 2.4.1.1 | metabolism |
glycogen degradation and synthesis during the diurnal cycle are mediated by changes in the activities of phosphorylase and glycogen synthase. Phosphorylase is regulated by phosphorylation of Ser14. Only the phosphorylated form of liver phosphorylase (GPa) is catalytically active. Interconversion between GPa and GPb (unphosphorylated) is dependent on the activities of phosphorylase kinase and of phosphorylase phosphatase. The latter comprises protein phosphatase-1 in conjunction with a glycogen-targeting protein (G-subunit) of the PPP1R3 family. Both GPa and phosphorylated glycogen synthase serve as substrates for the catalytic subunit of protein phosphatase-1 in association with G-subunits |
736773 |
| 2.4.1.1 | metabolism |
glycogen phosphorylase is a key enzyme involved in intracellular glycogen catabolism, catalyzing the first step in glycogen degradation. In the diapause, GPase catalyzes glycogen into the closely related molecule, sorbitol. The GPase gene expression is stress-related and might play an important role in Artemia development and metabolism |
736783 |
| 2.4.1.1 | metabolism |
glycogen synthase and glycogen phosphorylase are the two enzymes that control, respectively, the synthesis and degradation of this polysaccharide |
736933 |
| 2.4.1.1 | metabolism |
muscle glycogen phosphorylase is the rate-limiting enzyme of glycogen breakdown in skeletal muscle |
-, 736105 |
| 2.4.1.1 | more |
despite a high degree of conservation of residues between liver and muscle isoforms in the ligand binding residues at the catalytic and allosteric sites, the kinetic properties of liver phosphorylase differ from the muscle isoform |
736773 |
| 2.4.1.1 | more |
modeling of the glycogen phosphorylase b GPb receptor structure using the 2.15 A resolution GPb-N-4-phenylbenzoyl-2-N'-beta-D-glycopyrglycopyranosyl urea crystal complex, PDB ID 2QLN |
735773 |
| 2.4.1.1 | more |
phosphorylase a is produced and isolated utilizing purified phosphorylase b and commercially available phosphorylase kinase |
718873 |
| 2.4.1.1 | more |
structural analysis of molecular elements that govern molecular recognition by the catalytic site of the enzyme with emphasis in the beta-pocket environment, overview |
719413 |
