Membrane-associated phosphatidylinositol kinase from Saccharomyces cerevisiae

M. A. McKenzie, George Carman

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Membrane-associated phosphatidylinositol kinase (ATP:phosphatidylinositol 4-phosphotransferase, EC 2.7.1.67) was partially purified 93-fold from Saccharomyces cerevisiae. Activity was dependent on magnesium ions (10 mM) and the optimum pH was 8.5. The apparent K(m) values for ATP and phosphatidylinositol were 0.21 mM and 71 μM, respectively. Activity was stimulated by sodium cholate and inhibited by sodium, potassium, lithium, and fluoride ions.

Original languageEnglish (US)
Pages (from-to)421-423
Number of pages3
JournalJournal of bacteriology
Volume156
Issue number1
StatePublished - Jan 1 1983

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Phosphatidylinositols
Saccharomyces cerevisiae
Phosphotransferases
Adenosine Triphosphate
Sodium Cholate
Ions
1-Phosphatidylinositol 4-Kinase
Membranes
Magnesium
Sodium
potassium fluoride
lithium fluoride

All Science Journal Classification (ASJC) codes

  • Microbiology
  • Molecular Biology

Cite this

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Membrane-associated phosphatidylinositol kinase from Saccharomyces cerevisiae. / McKenzie, M. A.; Carman, George.

In: Journal of bacteriology, Vol. 156, No. 1, 01.01.1983, p. 421-423.

Research output: Contribution to journalArticle

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