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Literature summary for 2.4.1.1 extracted from

  • Tiraidis, C.; Alexacou, K.M.; Zographos, S.E.; Leonidas, D.D.; Gimisis, T.; Oikonomakos, N.G.
    FR258900, a potential anti-hyperglycemic drug, binds at the allosteric site of glycogen phosphorylase (2007), Protein Sci., 16, 1773-1782.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
AMP physiological activator Oryctolagus cuniculus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the cocrystallized rabbit muscle glycogen phosphorylase b–FR258900 complex, 2.2 A resolution Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
FR258900 the inhibitor binds at the allosteric activator site, where the physiological activator AMP binds. The contacts from FR258900 to glycogen phosphorylase are dominated by nonpolar van der Waals interactions with Gln71, Gln72, Phe196, and Val459 (from the symmetry-related subunit), and also by ionic interactions from the carboxylate groups to the three arginine residues (Arg242, Arg309, and Arg310) that form the allosteric phosphate-recognition subsite. The binding of FR258900 to the protein promotes conformational changes that stabilize an inactive T-state quaternary conformation of the enzyme Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00489
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycogen + glucose 1-phosphate
-
Oryctolagus cuniculus glycogen + phosphate
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00046
-
FR258900
-
Oryctolagus cuniculus

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0003
-
-
Oryctolagus cuniculus FR258900