Studies on the metabolism of ATP by isolated bacterial membranes

Solubilization and phosphorylation of a protein component of the diglyceride kinase system

Edwin Thomas, Herbert Weissbach, H. R. Kaback

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

A soluble fraction, obtained by extracting E. coli cytoplasmic membrane vesicles with water, transfers radioactivity from [γ-32P]ATP to a protein present in this soluble fraction. The formation of the [32P]phosphoprotein appears to be reversible. Thus the protein can transfer its 32P to ADP to form [32P]ATP, and the phosphate on the protein can exchange with the phosphate of ATP. Preliminary evidence indicates that the phosphate moiety is linked to a histidine residue of the protein. The Mn2+ and ATP dependencies of [32P]phosphoprotein formation are almost identical to the diglyceride kinase reaction previously reported in intact membrane vesicles. Although indirect evidence supports the involvement of the phosphoprotein in the diglyceride kinase reaction, the soluble fraction catalyzes only a slow formation of [32P]phosphatidie acid from [γ-32P]ATP and α,β-diglyceride.

Original languageEnglish (US)
Pages (from-to)327-333
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume157
Issue number2
DOIs
StatePublished - Jan 1 1973
Externally publishedYes

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Diacylglycerol Kinase
Phosphorylation
Metabolism
Adenosine Triphosphate
Phosphoproteins
Membranes
Phosphates
Proteins
Cytoplasmic Vesicles
Diglycerides
Radioactivity
Histidine
Adenosine Diphosphate
Escherichia coli
Cell Membrane
Acids
Water

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

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abstract = "A soluble fraction, obtained by extracting E. coli cytoplasmic membrane vesicles with water, transfers radioactivity from [γ-32P]ATP to a protein present in this soluble fraction. The formation of the [32P]phosphoprotein appears to be reversible. Thus the protein can transfer its 32P to ADP to form [32P]ATP, and the phosphate on the protein can exchange with the phosphate of ATP. Preliminary evidence indicates that the phosphate moiety is linked to a histidine residue of the protein. The Mn2+ and ATP dependencies of [32P]phosphoprotein formation are almost identical to the diglyceride kinase reaction previously reported in intact membrane vesicles. Although indirect evidence supports the involvement of the phosphoprotein in the diglyceride kinase reaction, the soluble fraction catalyzes only a slow formation of [32P]phosphatidie acid from [γ-32P]ATP and α,β-diglyceride.",
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AU - Kaback, H. R.

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