Application | Comment | Organism |
---|---|---|
additional information | the enzyme is a target for development of inhibitors to prevent unwanted hepatic glycogenolysis under high glucose conditions in treatment of diabetes type 2 in humans | Oryctolagus cuniculus |
Crystallization (Comment) | Organism |
---|---|
native enzyme crystals are soaked in 150 mM gamma-cyclodextrin, or 15 mM beta-cyclodextrin, respectively, and 70 mM maltopentaose or maltoheptaose in fesh solutions of mother liquor containing 10 mM MES, pH 6.7, 0.1 mM EDTA, at least 2 h at room temperature, X-ray diffraction structure determination and analysis of enzyme-inhibitor complexes at 2.3 A and 1.94 A resolution, respectively | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
alpha-cyclodextrin | mixed-type competitive inhibition, inhibitor is not bound into the enzyme crystal | Oryctolagus cuniculus | |
beta-cyclodextrin | mixed-type competitive inhibition, the inhibitor can be accomodated in the glycogen storage site of T-state enzyme, subsite specificity | Oryctolagus cuniculus | |
gamma-cyclodextrin | mixed-type competitive inhibition, the inhibitor can be accomodated in the glycogen storage site of T-state enzyme, subsite specificity | Oryctolagus cuniculus | |
additional information | binding and inhibition mechanism, no inhibition by (2,3,6-tri-O-methyl)-gamma-cyclodextrin | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate | determination and analysis of rgulatory binding sites | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Synonyms | Comment | Organism |
---|---|---|
glycogen phosphorylase | - |
Oryctolagus cuniculus |
GP | - |
Oryctolagus cuniculus |
GPb | - |
Oryctolagus cuniculus |
phosphorylase b | - |
Oryctolagus cuniculus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
7.4 | - |
gamma-cyclodextrin | with respect to glycogen | Oryctolagus cuniculus | |
14.1 | - |
beta-cyclodextrin | with respect to glycogen | Oryctolagus cuniculus | |
47.1 | - |
alpha-cyclodextrin | with respect to glycogen | Oryctolagus cuniculus |