Submitted on February 13, 2008
Revised on March 10, 2008
Accepted on March 27, 2008
Acyltransferases in bacterial glycerophospholipid synthesis
Yong-Mei Zhang and Charles O. Rock
Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105-2794
Corresponding Author: charles.rock{at}stjude.org
Phospholipid biosynthesis is a vital facet of bacterial physiology that begins with the synthesis of the fatty acids by a soluble type II fatty acid synthase. The bacterial glycerol-phosphate acyltransferases utilize the completed fatty acid chains to form the first membrane phospholipid, and thus play a critical role in the regulation of membrane biogenesis. The first bacterial acyltransferase described was PlsB, a glycerol-phosphate acyltransferase. PlsB is a key regulatory point that coordinates membrane phospholipid formation with cell growth and macromolecular synthesis. Phosphatidic acid is then produced by PlsC, a 1-acylglycerol-phosphate acyltransferase. These two acyltransferases use thioesters of either CoA or acyl carrier protein (ACP) as the acyl donors, and have homologs that perform the same reactions in higher organisms. However, the most prevalent glycerol-phosphate acyltransferase in the bacterial world is PlsY, which uses a recently discovered acyl-phosphate fatty acid intermediate as an acyl donor. This unique activated fatty acid is formed from the acyl-ACP end-products of the fatty acid biosynthetic pathway by PlsX, an acyl-ACP:phosphate transacylase.
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