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Structure and Regulation of the SN-Glycerol-3-Phosphate Acyltransferase of E. Coli

  • Robert M. Bell
  • Mark A. Scheideler
  • Bill Wilkison
Part of the NATO ASI Series book series (NSSA, volume 116)

Abstract

The cytoplasmic membrane bound acyl-Coenzyme A:sn-glycerol-3-phosphate(glycerol-P) O-acyltransferase(EC 2.3.1.15) of Escherichia coli catalyzes the initial committed step of membrane phospholipid biosynthesis. Phospholipid biosynthesis is likely regulated, in part, by this enzyme. Studies on glycerol-P acyltransferase were limited, until recently, to crude membrane preparations or partially purified preparations. Using a combined approach of molecular genetics and biochemistry, we have attempted to bring the study of the glycerol-P acyltransferase to a molecular level and establish a suitable system for in-depth functional and regulatory studies.

Keywords

Cyanogen Bromide Phospholipid Vesicle Acyltransferase Activity Phospholipid Biosynthesis Section Electron Microscopy 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Robert M. Bell
    • 1
  • Mark A. Scheideler
    • 1
  • Bill Wilkison
    • 1
  1. 1.Department of BiochemistryDuke University Medical CenterDurhamUSA

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