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Literature summary for 2.7.11.19 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
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
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

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

Metals/Ions

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

Organism

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

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
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Substrates and Products (Substrate)

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

Synonyms Comment Organism
PhK
-
 Oryctolagus cuniculus

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Oryctolagus cuniculus

General Information

General Information Comment Organism
metabolism the enzyme plays a key role in the cascade system for regulating glycogen metabolism Oryctolagus cuniculus
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