Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the nonactivated enzyme is activated either by limited proteolysis | Oryctolagus cuniculus | |
Trypsin | proteolytic activation of nonactivated enzyme | Oryctolagus cuniculus |
General Stability | Organism |
---|---|
Delta-Subunit remains tightly bound to alphagammadelta subunit complex even in the presence of 8 M urea | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
EGTA | together with trifluoperazime additive effect | Oryctolagus cuniculus | |
Trifluoperazine | nonspecific inactivation, at high concentrations, together with EGTA additive effect | Oryctolagus cuniculus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | effect of isolated delta subunit on kinetic parameters of nonactivated holoenzyme and alphagammadelta complex | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | requirement | Oryctolagus cuniculus | |
Mg2+ | major role of Mg2+: cosubstrate in Mg2+-ATP complex | Oryctolagus cuniculus | |
phosphate | requirement, phosphate containing enzyme | Oryctolagus cuniculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by affinity chromatography on calmodulin-Sepharose 4B | Oryctolagus cuniculus |
catalytically active alphagammadelta complexes | Oryctolagus cuniculus |
catalytically active gammadelta complexes | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + phosphorylase b | cosubstrate: Mg-ATP complex | Oryctolagus cuniculus | ADP + phosphorylase a | - |
? | |
ATP + synthetic pentadecapeptide | from amino-terminal of glycogen synthase, i.e. Pro-Leu-Ser-Arg-Thr-Leu-Ser-Val-Ser-Ser-Leu-Pro-Gly-Leu-Glu | Oryctolagus cuniculus | ? | - |
? | |
ATP + synthetic tetradecapeptide | i.e. Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Arg-Gly-Leu | Oryctolagus cuniculus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | molecular interaction and subunit structure | Oryctolagus cuniculus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
50% loss of nonactivated enzyme activity within 15 min, 50% loss of alphagammadelta subunit complex activity within 7 min, 90% loss of gammadelta subunit complex activity within 5 min | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Calmodulin | requirement | Oryctolagus cuniculus | |
Calmodulin | calmodulin containing enzyme i.e. tightly bound delta subunit | Oryctolagus cuniculus | |
Calmodulin | activation of nonactivated enzyme and alphagammadelta subunit complex | Oryctolagus cuniculus | |
Calmodulin | interacts with alpha subunit | Oryctolagus cuniculus |