Activating Compound | Comment | Organism | Structure |
---|---|---|---|
cAMP | dependent on | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
FAD | FAD at high concentrations completely inhibits the second stage of enzyme binding to glycogen particles containing glycogen phosphorylase b, the inhibitory effect of FAD is not complete and reaches a maximal value at FAD concentrations around 0.03 mM | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required for activity | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
DEAE Toyopearl 650M column chromatography | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + glycogen phosphorylase b | PhK catalyzes the Ca2+- and cAMP-dependent glycogen phosphorylase b phosphorylation and activation | Oryctolagus cuniculus | ADP + phosphorylated glycogen phosphorylase b | - |
? |
Synonyms | Comment | Organism |
---|---|---|
EC 2.7.1.38 | formerly | Oryctolagus cuniculus |
PhK | - |
Oryctolagus cuniculus |
phosphorylase kinase | - |
Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Oryctolagus cuniculus |