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Literature summary extracted from

  • Miyagawa, D.; Makino, Y.; Sato, M.
    Sensitive, nonradioactive assay of phosphorylase kinase through measurement of enhanced phosphorylase activity towards fluorogenic dextrin (2016), J. Biochem., 159, 239-246.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.19 glycogen significantly stimulates the enzyme PhK. GPb molecules located on the glycogen surface might serve as good connecting molecules between PhK and glycogen and, consequently, promote indirect binding of PhK to the glycogen surface. Under conditions of high ionic strength and high ATP concentration in the body, direct binding of PhK to glycogen is reported to be very weak. The ternary PhK-GPbn-glycogen complex produces active GPa very efficiently compared with PhK, either alone or in the binary complex, i.e. the PhK-GPb complex. The effect is inhibited by gamma-cyclodextrin Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.19 ATP enzyme PhK shows substrate inhibition at high ATP concentration above 3 mM Oryctolagus cuniculus
2.7.11.19 EDTA complete inhibition at 50 mM Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.19 Ca2+ required Oryctolagus cuniculus
2.7.11.19 Mg2+ required 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
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 2 ADP + glycogen phosphorylase a
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.19 Oryctolagus cuniculus P18688 AND P12798 subunits a and b
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.19 skeletal muscle
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 Oryctolagus cuniculus
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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
-
 ?
2.7.11.19 2 ATP + glycogen phosphorylase b rabbit muscle GP Oryctolagus cuniculus 2 ADP + glycogen phosphorylase a
-
 ?
2.7.11.19 additional information development of a highly sensitive and nonradioactive assay for phosphorylase kinase activity by measuring the enhanced glycogen phosphorylase activity towards a pyridylaminated maltohexaose, method evaluation, phosphate quantification by the FiskeSubbarow method, overview Oryctolagus cuniculus ?
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 ?

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 37
-
 assay at Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.19 8.2
-
 assay at Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.19 ATP
-
 Oryctolagus cuniculus

General Information

EC Number General Information Comment Organism
2.7.11.19 metabolism the enzyme plays a key role in the cascade system for regulating glycogen metabolism Oryctolagus cuniculus
2.7.11.19 physiological function glycogen phosphorylase, EC 2.4.1.1, exists in two interconvertible forms, GPa (phosphorylated form, high activity) and GPb (nonphosphorylated form, low activity). Phosphorylase kinase catalyses the phosphorylation of GPb and plays a key role in the cascade system for regulating glycogen metabolism Oryctolagus cuniculus