The Enzyme Database

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EC 2.3.1.274     
Accepted name: phosphate acyltransferase
Reaction: an acyl-[acyl-carrier protein] + phosphate = an acyl phosphate + an [acyl-carrier protein]
Other name(s): plsX (gene name); acyl-ACP phosphotransacylase; acyl-[acyl-carrier-protein]—phosphate acyltransferase; phosphate-acyl-ACP acyltransferase
Systematic name: an acyl-[acyl-carrier protein]:phosphate acyltransferase
Comments: The enzyme, found in bacteria, catalyses the synthesis of fatty acyl-phosphate from acyl-[acyl-carrier protein], a step in the most widely distributed bacterial pathway for the initiation of phospholipid formation. While the activity is modestly enhanced by Mg2+, the enzyme does not require a divalent cation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Lu, Y.J., Zhang, Y.M., Grimes, K.D., Qi, J., Lee, R.E. and Rock, C.O. Acyl-phosphates initiate membrane phospholipid synthesis in Gram-positive pathogens. Mol. Cell 23 (2006) 765–772. [PMID: 16949372]
2.  Yoshimura, M., Oshima, T. and Ogasawara, N. Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol. 7:69 (2007). [PMID: 17645809]
3.  Kim, Y., Li, H., Binkowski, T.A., Holzle, D. and Joachimiak, A. Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis. J Struct Funct Genomics 10 (2009) 157–163. [PMID: 19058030]
4.  Kaczmarzyk, D., Cengic, I., Yao, L. and Hudson, E.P. Diversion of the long-chain acyl-ACP pool in Synechocystis to fatty alcohols through CRISPRi repression of the essential phosphate acyltransferase PlsX. Metab. Eng. 45 (2018) 59–66. [PMID: 29199103]
[EC 2.3.1.274 created 2018]
 
 


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