Literature summary extracted from
Eronina, T.B.; Chebotareva, N.A.; Sluchanko, N.N.; Mikhaylova, V.V.; Makeeva, V.F.; Roman, S.G.; Kleymenov, S.Y.; Kurganov, B.I.
Dual effect of arginine on aggregation of phosphorylase kinase (2014), Int. J. Biol. Macromol., 68, 225-232.
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.11.19 |
Ca2+ |
dependent on |
Oryctolagus cuniculus |
|
2.7.11.19 |
Mg2+ |
required |
Oryctolagus cuniculus |
|
2.7.11.19 |
additional information |
Ca2+ and Mg2+ induce self-aggregation of PhK at 37°C |
Oryctolagus cuniculus |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.11.19 |
2 ATP + glycogen phosphorylase b |
Oryctolagus cuniculus |
- |
2 ADP + glycogen phosphorylase a |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.11.19 |
Oryctolagus cuniculus |
P18688 AND P12798 |
subunits a and b |
- |
Source Tissue
EC Number |
Source Tissue |
Comment |
Organism |
Textmining |
---|
2.7.11.19 |
skeletal muscle |
- |
Oryctolagus cuniculus |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.11.19 |
2 ATP + glycogen phosphorylase b |
- |
Oryctolagus cuniculus |
2 ADP + glycogen phosphorylase a |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.11.19 |
hexadecamer |
(alphabetagammadelta)4 |
Oryctolagus cuniculus |
2.7.11.19 |
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
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.11.19 |
PhK |
- |
Oryctolagus cuniculus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.7.11.19 |
25 |
37 |
assay at |
Oryctolagus cuniculus |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.7.11.19 |
6.8 |
- |
assay at |
Oryctolagus cuniculus |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.11.19 |
physiological function |
the enzyme is a Ca2+-dependent regulatory enzymethat catalyzes phosphorylation and activation of glycogen phosphorylase b |
Oryctolagus cuniculus |