Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | dependent on | Oryctolagus cuniculus | |
Mg2+ | required | Oryctolagus cuniculus | |
additional information | Ca2+ and Mg2+ induce self-aggregation of PhK at 37°C | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + glycogen phosphorylase b | Oryctolagus cuniculus | - |
2 ADP + glycogen phosphorylase a | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P18688 AND P12798 | subunits a and b | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ATP + glycogen phosphorylase b | - |
Oryctolagus cuniculus | 2 ADP + glycogen phosphorylase a | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexadecamer | (alphabetagammadelta)4 | Oryctolagus cuniculus |
More | Ca2+and Mg2+ions induce the self-association of PhK. Effects of arginine on protein-protein interactions in the enzyme polymer: arginine induces aggregation of Ca2+-free enzyme PhK. But when studying Ca2+, Mg2+-induced aggregation of PhK at 37°C, the protective effect of arginine is demon-strated, disruption of PhK hexadecameric structure occurs under the action of arginine. Although HspB6 and HspB5 suppress aggregation of PhK they do not block the disruption effect of arginine with respect to both forms of PhK (Ca2+-free and Ca2+, Mg2+-bound conformers). Aggregation of PhK induced by 0.5 M Arg is significantly suppressed in the presence of 1 M trimethylamine N-oxide dihydrate (TMAO) | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
PhK | - |
Oryctolagus cuniculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 37 | assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.8 | - |
assay at | Oryctolagus cuniculus |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is a Ca2+-dependent regulatory enzymethat catalyzes phosphorylation and activation of glycogen phosphorylase b | Oryctolagus cuniculus |