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Literature summary for 2.7.11.19 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.
    View publication on PubMed

Metals/Ions

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Oryctolagus cuniculus P18688 AND P12798 subunits a and b
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ATP + glycogen phosphorylase b
-
Oryctolagus cuniculus 2 ADP + glycogen phosphorylase a
-
?

Subunits

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

Synonyms Comment Organism
PhK
-
Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25 37 assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Oryctolagus cuniculus

General Information

General Information Comment Organism
physiological function the enzyme is a Ca2+-dependent regulatory enzymethat catalyzes phosphorylation and activation of glycogen phosphorylase b Oryctolagus cuniculus