|Gene:||plsB||Accession Numbers: EG10740 (EcoCyc), b4041, ECK4033|
Synonyms: sn-glycerol-3-phosphate acyltransferase, GPAT, glycerolphosphate acyltransferase, glycerol-3-phosphate O-acyltransferase
Membrane-bound glycerol-3-phosphate acyltransferase (PlsB) catalyzes the first committed step in phospholipid biosynthesis and is thought to function in close proximity to the succeeding enzyme 1-acylglycerol-3-phosphate O-acyltransferase (PlsC) [Kessels83]. It is specific for acylation at position 1 of sn-glycerol 3-phosphate and can utilize either fatty acyl-acyl carrier protein (acyl-ACP) or fatty acyl-coenzyme A (acyl-CoA) thioesters as acyl donors to form a 1-acyl-sn-glycerol 3-phosphate. Fatty acids that are endogenously synthesized are attached to ACP and exogenously added fatty acids are attached to CoA [Ishinaga76, Snider77, Larson80, Lightner80, Rock81, Green81, Greenway83, Wilkison86, Ray87]. In E. coli phospholipids the sn 1 position is occupied mainly by either palmitate, or cis-vaccenate, whereas the sn 2 position is predominantly palmitoleate, or cis-vaccenate. This is thought to result from the substrate preferences of the PlsB and PlsC enzymes [Rock81, Goelz80].
The plsB gene has been shown to be regulated by stress response regulators such as RNA polymerase, sigma 24 (sigma E) factor and ppGpp [Heath94, Rhodius05, Wahl09, Wahl11]. PlsB is part of a protein network for phospholipid synthesis and interacts with a holo-[acyl-carrier protein] (ACP), esterase/thioesterase (YbgC) and phosphatidylserine synthase (PssA) to form a complex at the cytoplasmic side of the inner membrane [Gully06].
Site-directed mutagenesis and chemical modification studies have demonstrated catalytically important amino acid residues in PlsB, including an invariant histidine residue that is essential for catalysis [Heath98, Lewin99]. Genetic studies have identified the plsB locus as involved in the formation of multidrug tolerant persister cells [Spoering06].
The properties of the E. coli B enzyme were studied in earlier work [Kito72, Okuyama73,
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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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