Thiophosphate-activated phosphorylase kinase as a probe in the regulation of phosphorylase phosphatase

P. Gergely, G. Vereb, György Bot

Research output: Contribution to journalArticle

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Abstract

Rabbit muscle nonactivated phosphorylase kinase (EC 2.7.1.38) is converted to thiophosphate-activated phosphorylase kinase by cyclic AMP dependent protein kinase, Mg2+ and ATP-γ-S /adenosine-5′-O-(s-thiotriphosphate)/. The formation of thiophosphate-activated phosphorylase kinase was also observed in the protein-glycogen complex from skeletal muscle. This new form of kinase is resistant to the action of phosphatase and behaves as a competitive inhibitor in the dephosphorylation of phosphorylase a by phosphorylase phosphatase (Ki = 0.04 mg per ml). The fact that the inhibitory effect of thiophosphate-activated phosphorylase kinase is 3 times higher than in the case of nonactivated kinase, may explain the transient inhibition of phosphorylase phosphatase in the protein-glycogen complex. The use of activated (phosphorylated) phosphorylase kinase supports this assumption since it causes a delay in the dephosphorylation of phosphorylase a, i.e. the conversion of phosphorylase a into b could start only after the dephosphorylation of activated phosphorylase kinase.

Original languageEnglish
Pages (from-to)809-816
Number of pages8
JournalBBA - Enzymology
Volume429
Issue number3
DOIs
Publication statusPublished - May 13 1976

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Phosphorylase Phosphatase
Phosphorylase Kinase
Phosphorylase a
Glycogen
Phosphotransferases
Cyclic AMP-Dependent Protein Kinases
Phosphoric Monoester Hydrolases
thiophosphoric acid
Skeletal Muscle
Proteins
Adenosine Triphosphate
Rabbits
Muscles

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Thiophosphate-activated phosphorylase kinase as a probe in the regulation of phosphorylase phosphatase. / Gergely, P.; Vereb, G.; Bot, György.

In: BBA - Enzymology, Vol. 429, No. 3, 13.05.1976, p. 809-816.

Research output: Contribution to journalArticle

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AB - Rabbit muscle nonactivated phosphorylase kinase (EC 2.7.1.38) is converted to thiophosphate-activated phosphorylase kinase by cyclic AMP dependent protein kinase, Mg2+ and ATP-γ-S /adenosine-5′-O-(s-thiotriphosphate)/. The formation of thiophosphate-activated phosphorylase kinase was also observed in the protein-glycogen complex from skeletal muscle. This new form of kinase is resistant to the action of phosphatase and behaves as a competitive inhibitor in the dephosphorylation of phosphorylase a by phosphorylase phosphatase (Ki = 0.04 mg per ml). The fact that the inhibitory effect of thiophosphate-activated phosphorylase kinase is 3 times higher than in the case of nonactivated kinase, may explain the transient inhibition of phosphorylase phosphatase in the protein-glycogen complex. The use of activated (phosphorylated) phosphorylase kinase supports this assumption since it causes a delay in the dephosphorylation of phosphorylase a, i.e. the conversion of phosphorylase a into b could start only after the dephosphorylation of activated phosphorylase kinase.

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