This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
|Superclasses:||Biosynthesis → Fatty Acids and Lipids Biosynthesis → Phospholipid Biosynthesis → CDP-diacylglycerol Biosynthesis|
Phospholipids are important membrane components. Most of the phospholipids belong to the category of phosphoglycerides. The simplest phosphoglycerides, which are known as phosphatidates, are composed of a glycerol molecule attached to two fatty acids and one phosphate group. The carboxyl group of each fatty acid is esterified to the hydroxyl groups on carbon-1 and carbon-2 of the glycerol molecule, while the phosphate group is attached to carbon-3 by an ester link. Phosphatidates are precursors for many phosphoglycerides found in animals, plants and yeast, including a phosphatidylinositol, an L-1-phosphatidylserine, an L-1-phosphatidyl-ethanolamine, and a cardiolipin.
As part of the synthesis of phosphoglycerides, either the phosphatidate or the modifying compound need to be activated by CTP. In some cases, the modifying compound is activated, as in the case of choline and ethanolamine, which form CDP-choline and CDP-ethanolamine, respectively. However, in the case of other compounds, such as L-serine and myo-inositol, the phosphatidate is activated first, forming a CDP-diacylglycerol, which then reacts with the modifying compound to form the phosphoglyceride.
About This Pathway
This pathway describes the biosynthesis of a CDP-diacylglycerol in some Gram-negative bacteria (primarily the Gammaproteobacteria) as well as the chloroplasts of green plants. In this pathway the production of the intermediate a 1-acyl-sn-glycerol 3-phosphate is catalyzed by a type of the membrane-bound enzyme glycerol-3-phosphate acyltransferase that uses an acyl-[acyl-carrier protein] as the acyl donor.
Bacteria enzymes that can utilze an acyl-[acyl-carrier protein] are found only in some Gram-negative bacteria. They are encoded by the plsB gene, and can also utilize a long-chain acyl-CoA thioesters. The plasitidic enzyme can use only an acyl-[acyl-carrier protein] [Murata97].
The addition of the second acyl moiety is catalyzed by 1-acylglycerol-3-phosphate O-acyltransferase. The bacterial enzyme, which is universally expressed in all bacteria, is encoded by plsC. As in the case of PlsB, it can utilize either a fatty acyl-[acp] or an acyl-CoA thioester as the acyl donor.
A pathway that describes the usage of acyl-CoA donors can be found at CDP-diacylglycerol biosynthesis I. It should be noted that most bacteria utilize a different route for the synthesis of a 1-acyl-sn-glycerol 3-phosphate, as described in CDP-diacylglycerol biosynthesis III.
More information can be found in phospholipid biosynthesis II.
Unification Links: EcoCyc:PWY0-1319
Xu06: Xu C, Yu B, Cornish AJ, Froehlich JE, Benning C (2006). "Phosphatidylglycerol biosynthesis in chloroplasts of Arabidopsis mutants deficient in acyl-ACP glycerol-3- phosphate acyltransferase." Plant J 47(2);296-309. PMID: 16774646
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
Bayan89: Bayan N, Therisod H (1989). "Evidence for interactions of acyl carrier protein with glycerol-3-phosphate acyltransferase, an inner membrane protein of Escherichia coli." FEBS Lett 1989;255(2);330-4. PMID: 2676605
Bell74: Bell RM (1974). "Mutants of Escherichia coli defective in membrane phospholipid synthesis: macromolecular synthesis in an sn-glycerol 3-phosphate acyltransferase Km mutant." J Bacteriol 117(3);1065-76. PMID: 4591941
Bell75: Bell RM, Cronan JE (1975). "Mutants of Escherichia coli defective in membrane phospholipid synthesis. Phenotypic suppression of sn-glycerol-3-phosphate acyltransferase Km mutants by loss of feedback inhibition of the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 250(18);7153-8. PMID: 240817
Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043
Chen08: Chen YQ, Kuo MS, Li S, Bui HH, Peake DA, Sanders PE, Thibodeaux SJ, Chu S, Qian YW, Zhao Y, Bredt DS, Moller DE, Konrad RJ, Beigneux AP, Young SG, Cao G (2008). "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase." J Biol Chem 283(15);10048-57. PMID: 18238778
Clark80: Clark D, Lightner V, Edgar R, Modrich P, Cronan JE, Bell RM (1980). "Regulation of phospholipid biosynthesis in Escherichia coli. Cloning of the structural gene for the biosynthetic sn-glycerol-3-phosphate dehydrogenase." J Biol Chem 255(2);714-7. PMID: 6985897
Cronan74: Cronan JE, Bell RM (1974). "Mutants of Escherichia coli defective in membrane phospholipid synthesis: mapping of the structural gene for L-glycerol 3-phosphate dehydrogenase." J Bacteriol 118(2);598-605. PMID: 4597451
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
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