Membrane-associated phosphatidylinositol kinase from Saccharomyces cerevisiae

J Bacteriol. 1983 Oct;156(1):421-3. doi: 10.1128/jb.156.1.421-423.1983.

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 Km values for ATP and phosphatidylinositol were 0.21 mM and 71 microM, respectively. Activity was stimulated by sodium cholate and inhibited by sodium, potassium, lithium, and fluoride ions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 1-Phosphatidylinositol 4-Kinase
  • Adenosine Triphosphate / metabolism
  • Cholic Acid
  • Cholic Acids / pharmacology
  • Hydrogen-Ion Concentration
  • Kinetics
  • Magnesium / pharmacology
  • Magnesium Chloride
  • Microsomes / enzymology
  • Phosphatidylinositols / metabolism
  • Phosphotransferases / isolation & purification
  • Phosphotransferases / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins*

Substances

  • Cholic Acids
  • Phosphatidylinositols
  • Saccharomyces cerevisiae Proteins
  • Magnesium Chloride
  • Adenosine Triphosphate
  • Phosphotransferases
  • 1-Phosphatidylinositol 4-Kinase
  • PIK1 protein, S cerevisiae
  • Cholic Acid
  • Magnesium