Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, in the presence of 1 M trimethylamine-N-oxide, FAD has an inhibitory effect on self-association of phosphorylase kinase | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of phosphorylase kinase-glycogen complex formation | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required for complex formation | Oryctolagus cuniculus | |
Mg2+ | required for complex formation and activity | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + glycogen phosphorylase b | Oryctolagus cuniculus | - |
ADP + phosphorylated glycogen phosphorylase b | - |
? | |
additional information | Oryctolagus cuniculus | interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from skeletal muscle by anion exchange chromatography to homogeneity | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + glycogen phosphorylase b | - |
Oryctolagus cuniculus | ADP + phosphorylated glycogen phosphorylase b | - |
? | |
additional information | interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle | Oryctolagus cuniculus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
26 | - |
assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Oryctolagus cuniculus |