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Literature summary for 2.4.1.1 extracted from

  • Hadjiloi, T.; Tiraidis, C.; Chrysina, E.D.; Leonidas, D.D.; Oikonomakos, N.G.; Tsipos, P.; Gimisis, T.
    Binding of oxalyl derivatives of beta-d-glucopyranosylamine to muscle glycogen phosphorylase b (2006), Bioorg. Med. Chem., 14, 3872-3882.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with inhibitors beta-D-glucopyranosyl 1-oxalylamide, beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide, beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide. Inhibitors accomodate at the catalytic site at approximately the position of alpha-D-glucose and stabilize the T-state conformation Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide competitive Oryctolagus cuniculus
beta-D-glucopyranosyl 1-(ethoxy(oxo)acetyl)-amide competitive Oryctolagus cuniculus
beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide competitive Oryctolagus cuniculus
beta-D-glucopyranosyl 1-oxalylamide competitive Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
muscle
-
Oryctolagus cuniculus
-

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.21
-
beta-D-glucopyranosyl 1-(methoxy(oxo)acetyl)-amide
-
Oryctolagus cuniculus
0.71
-
beta-D-glucopyranosyl 1-oxalylamide
-
Oryctolagus cuniculus
0.92
-
beta-D-glucopyranosyl 1-(ethoxy(oxo)acetyl)-amide
-
Oryctolagus cuniculus
1
-
beta-D-glucopyranosyl 1-(2-cyclopropylamino-2-oxoacetyl)-amide
-
Oryctolagus cuniculus