(1)       Rock, C. O., Goelz, S. E., Cronan, J. E., 1981. Phospholipid synthesis in Escherichia coli. Characteristics of fatty acid transfer from acyl-acyl carrier protein to sn-glycerol 3-phosphate. J. Biol. Chem. 256: 736–742.

(2)       Ray, T. K., Cronan, J. E., 1987. Acylation of glycerol 3-phosphate is the sole pathway of de novo phospholipid synthesis in Escherichia coli. Journal of Bacteriology 169: 2896–2898.

(3)       Shindou, H., Shimizu, T., 2009. Acyl-CoA:Lysophospholipid Acyltransferases. J. Biol. Chem. 284: 1–5.

(4)       Yao, J., Rock, C. O., 2013. Phosphatidic acid synthesis in bacteria. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, Phospholipids and phospholipid metabolism 1831: 495–502.

(5)       Protein Data Bank. https://www.rcsb.org/structure/5KYM.

(6)       Agarwal, A. K., 2012. Lysophospholipid acyltransferases: 1-acylglycerol-3-phosphate O-acyltransferases. From discovery to disease. Current Opinion in Lipidology 23: 290.

(7)       Robertson, R. M., et al., 2017. A two-helix motif positions the lysophosphatidic acid acyltransferase active site for catalysis within the membrane bilayer. Nature Structural & Molecular Biology 24: 666–671.

(8)       Protein identification and analysis tools on the ExPASy server. Gasteiger, E. et. al. In J. M. Walker (Ed.) The proteomics protocols handbook. Totowa, New Jersey: Humana Press Inc. 2005.

(9)       Basic Local Alignment Search Tool. National Center for Biotechnology Information. 2012. http://www.ncbi.nlm.nih.gov/blast/Blast.cgi.

(10)     Dali server: conservation mapping in 3D. Nucl. Acids Res. 38, W545-549. Holm L, Rosenström, P. 2010.

(11)     Protein Data Bank. https://www.rcsb.org/structure/1IUQ.

(12)     Tamada, T., et al., 2004. Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata and Spinacea oleracea. Acta Cryst D 60: 13–21.