HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bell, R. M. Search for Related Content PubMed PubMed Citation Articles by Bell, R. M. Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 18, 7147-7152, Sep, 1975

Mutants of Escherichia coli defective in membrane phospholipid synthesis. Properties of wild type and Km defective sn-glycerol-3-phosphate acyltransferase activities

R. M. Bell

The sn-glycerol-3-phosphate (glycerol-P) acyltransferase, the first enzyme of membrane phospholipid synthesis in Escherichia coli, was investigated in a wild type and a mutant strain defective in this activity. The mutant strain, selected as a glycerol-P auxotroph, was previously shown to contain a glycerol-P acyltransferase activity with an apparent Km for glycerol-P 10 times higher than that of its parent or revertants. The membranous mutant glycerol-P acyltransferase but did not appear to be thermolabile in vivo. Revertants no longer requiring glycerol-P for growth, showed glycerol-P acyltransferase activity with thermolability properties similar to the wild type. The second phospholipid biosynthetic enzyme, 1-acylglycerol-P acyltransferase, was not thermolabile in membranes containing a thermolabile glycerol-P acyltransferase activity. The pH optimum for the mutant acyltransferase was over 1 pH unit higher than that of the parental activity. Further, the mutant and wild type glycerol-P acyltransferase differed in their response to magnesium chloride and potassium chloride. The palmitoyl-CoA dependence of the wild type and mutant glycerol-P acyltransferase activities were different. The mutant glycerol-P acyltransferase activity was inhibited greater than 90% by Triton X-100 under conditions where the wild type activity was not affected. These experiments provide novel information about the wild type glycerol-P acyltransferase activity of E. coli and provide six additional lines of evidence for the mutant character of the glycerol-P acyltransferase in the mutant strains.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				Y.-M. Zhang and C. O. Rock Thematic Review Series: Glycerolipids. Acyltransferases in bacterial glycerophospholipid synthesis J. Lipid Res., September 1, 2008; 49(9): 1867 - 1874. [Abstract] [Full Text] [PDF]

				L. Paoletti, Y.-J. Lu, G. E. Schujman, D. de Mendoza, and C. O. Rock Coupling of Fatty Acid and Phospholipid Synthesis in Bacillus subtilis J. Bacteriol., August 15, 2007; 189(16): 5816 - 5824. [Abstract] [Full Text] [PDF]

				Y.-J. Lu, F. Zhang, K. D. Grimes, R. E. Lee, and C. O. Rock Topology and Active Site of PlsY: THE BACTERIAL ACYLPHOSPHATE:GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE J. Biol. Chem., April 13, 2007; 282(15): 11339 - 11346. [Abstract] [Full Text] [PDF]

				R. J. Heath and C. O. Rock A Missense Mutation Accounts for the Defect in the Glycerol-3-Phosphate Acyltransferase Expressed in the plsB26 Mutant J. Bacteriol., March 15, 1999; 181(6): 1944 - 1946. [Abstract] [Full Text]