Studies on the metabolism of ATP by isolated bacterial membranes

Formation and metabolism of membrane-bound phosphatidic acid

Herbert Weissbach, Edwin Thomas, H. R. Kaback

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Isolated E. coli membrane vesicles readily incorporate the terminal phosphate of ATP, and to a lesser degree, GTP, into phosphatidic acid. The reaction shows an absolute dependency for Mn ion, and the apparent Km values for ATP and Mn2+ were calculated to be 1.3 × 10-7 m and 3 × 10-5 m, respectively. The metabolism of the 32P-labeled membrane-bound phosphatidic acid has also been investigated. After incubating the labeled membranes with unlabeled ATP and ADP, [32P]ATP is formed in addition to 32P inorganic phosphate.

Original languageEnglish (US)
Pages (from-to)249-254
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume147
Issue number1
DOIs
StatePublished - Jan 1 1971
Externally publishedYes

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Phosphatidic Acids
Metabolism
Adenosine Triphosphate
Membranes
Phosphates
Guanosine Triphosphate
Adenosine Diphosphate
Escherichia coli
Ions

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Studies on the metabolism of ATP by isolated bacterial membranes : Formation and metabolism of membrane-bound phosphatidic acid. / Weissbach, Herbert; Thomas, Edwin; Kaback, H. R.

In: Archives of Biochemistry and Biophysics, Vol. 147, No. 1, 01.01.1971, p. 249-254.

Research output: Contribution to journalArticle

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