Phospholipase A and acyltransferase 2

Definition:

Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. For most substrates, PLA1 activity is much higher than PLA2 activity. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid. Shows N-acyltransferase activity, catalyzing the calcium-independent transfer of a fatty acyl group at the sn-1 position of phosphatidylcholine (PC) and other glycerophospholipids to the primary amine of phosphatidylethanolamine (PE), forming N-acylphosphatidylethanolamine (NAPE), which serves as precursor for N-acylethanolamines (NAEs). Catalyzes N-acylation of PE using both sn-1 and sn-2 palmitoyl groups of PC as acyl donor. Exhibits high phospholipase A1/2 activity and low N-acyltransferase activity.

References:

[1]. Emily B Mardian, et al. The HRASLS (PLA/AT) subfamily of enzymes. J Biomed Sci. 2015 Oct 26;22:99. [Content Brief]

[2]. Marcin Golczak, et al. Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. J Biol Chem. 2012 Jul 6;287(28):23790-807. [Content Brief]

[3]. Toru Uyama, et al. Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes. Biochim Biophys Acta. 2009 Dec;1791(12):1114-24. [Content Brief]

[4]. Toru Uyama, et al. Generation of N-acylphosphatidylethanolamine by members of the phospholipase A/acyltransferase (PLA/AT) family. J Biol Chem. 2012 Sep 14;287(38):31905-19. [Content Brief]

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