Reversible inhibition of skeletal muscle phosphoprotein phosphatase by ATP, phosphate and fluoride

Balwant S. Khatra, Thomas Soderling

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

A phosphoprotein phosphatase preparation which showed activity towards glycogen synthase, phosphorylase, phosphorylase kinase, and phosphohistones was reversibly inhibited (70-90%) by preincubation with free ATP (apparent Ki about 0.3 mM). Other nucleotides (ADP2 (apparent Ka 3μM) prior to assay. Other divalent metals (Co++ > Zn++ > Mg++) were partially effective in reversing the inhibition. It is concluded that ATP by virtue of its special structure and metal binding capacity possibly removes a catalytically important metal ion from the enzyme.

Original languageEnglish (US)
Pages (from-to)647-654
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume85
Issue number2
DOIs
StatePublished - Nov 29 1978
Externally publishedYes

Fingerprint

Phosphoprotein Phosphatases
Fluorides
Muscle
Skeletal Muscle
Adenosine Triphosphate
Metals
Phosphates
Phosphorylase Kinase
Glycogen Synthase
Phosphorylases
Metal ions
Glycogen Phosphorylase
Assays
Nucleotides
Enzymes
Ions

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Reversible inhibition of skeletal muscle phosphoprotein phosphatase by ATP, phosphate and fluoride. / Khatra, Balwant S.; Soderling, Thomas.

In: Biochemical and Biophysical Research Communications, Vol. 85, No. 2, 29.11.1978, p. 647-654.

Research output: Contribution to journalArticle

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