FUNCTION OF PHOSPHATIDYLGLYCEROL MOLECULAR-SPECIES IN MEMBRANES - ACTIVATION OF MEMBRANE-BOUND SN-GLYCEROL 3-PHOSPHATE ACYLTRANSFERASE IN ESCHERICHIA-COLI

  • 1 January 1976
    • journal article
    • research article
    • Vol. 431  (3) , 426-432
Abstract
Sn-Glycerol 3-phosphate acyltransferase (EC 2.3.1.15) bound to the elaidate-enriched membranes of an unsaturated fatty acid auxotroph of E. coli had a lower specific activity than the acyltransferase associated with the wild-type membranes. The 1-saturated-2-cis-unsaturated and 1,2-di-cis-unsaturated molecular species of phosphatidylglycerol activated this enzyme. These molecular species did not change the original temperature profile obtained by Arrhenius plots of the enzyme activity bound to the elaidate-enriched membranes.

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