Studies on the metabolism of ATP by isolated bacterial membranes

Role of succinyl CoA synthetase in diglyceride kinase activity

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1 Citation (Scopus)

Abstract

The diglyceride kinase activity of isolated E. coli membrane vesicles appears to be mediated in part by succinyl CoA synthetase. Upon incubation of vesicles with [γ-32P]ATP, or with 32Pi and succinyl CoA, radioactivity appears in membrane-bound phosphatidic acid. CoA inhibits incorporation of radioactivity from [γ-32P]ATP. Succinate lowers the concentration of CoA required to inhibit this incorporation, although succinate alone stimulates incorporation. At high [γ-32P]ATP concentrations, inhibition by succinate and CoA is overcome. The results suggest that diglyceride kinase can use either ATP or the phosphorylated form of succinyl CoA synthetase as phosphate donor for the phosphorylation of diglyceride.

Original languageEnglish (US)
Pages (from-to)530-536
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume163
Issue number2
DOIs
StatePublished - Jan 1 1974
Externally publishedYes

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Succinate-CoA Ligases
Diacylglycerol Kinase
Metabolism
Succinic Acid
Coenzyme A
Adenosine Triphosphate
Membranes
Radioactivity
Phosphatidic Acids
Phosphorylation
Diglycerides
Escherichia coli
Phosphates

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

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title = "Studies on the metabolism of ATP by isolated bacterial membranes: Role of succinyl CoA synthetase in diglyceride kinase activity",
abstract = "The diglyceride kinase activity of isolated E. coli membrane vesicles appears to be mediated in part by succinyl CoA synthetase. Upon incubation of vesicles with [γ-32P]ATP, or with 32Pi and succinyl CoA, radioactivity appears in membrane-bound phosphatidic acid. CoA inhibits incorporation of radioactivity from [γ-32P]ATP. Succinate lowers the concentration of CoA required to inhibit this incorporation, although succinate alone stimulates incorporation. At high [γ-32P]ATP concentrations, inhibition by succinate and CoA is overcome. The results suggest that diglyceride kinase can use either ATP or the phosphorylated form of succinyl CoA synthetase as phosphate donor for the phosphorylation of diglyceride.",
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AB - The diglyceride kinase activity of isolated E. coli membrane vesicles appears to be mediated in part by succinyl CoA synthetase. Upon incubation of vesicles with [γ-32P]ATP, or with 32Pi and succinyl CoA, radioactivity appears in membrane-bound phosphatidic acid. CoA inhibits incorporation of radioactivity from [γ-32P]ATP. Succinate lowers the concentration of CoA required to inhibit this incorporation, although succinate alone stimulates incorporation. At high [γ-32P]ATP concentrations, inhibition by succinate and CoA is overcome. The results suggest that diglyceride kinase can use either ATP or the phosphorylated form of succinyl CoA synthetase as phosphate donor for the phosphorylation of diglyceride.

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