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. 2017 Nov 17;7:15767. doi: 10.1038/s41598-017-16116-8

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Odd-chain acyl-CoAs are substrates of hLPCAT1 and CT775. Human long-chain acyl-CoA synthetase 6 (hACSL6) was purified and used to produce CoA in the ester form from 17-methyl-stearic acid (MeC₁₈-OH). MeC₁₈-CoA was purified on a Lipidex-1000 column (see Methods), and its ability to compete with the acylation of 1-acyl-GPC from NBD-C₁₆-CoA by human LPCAT1 (panel A) and CT775 (panel B) was determined. Measurements were performed with 0.5 µg of hLPCAT1 or CT775 microsomes in the presence of 20 µM 1-C₁₆-GPC and 0.5 µM NBD-C₁₆-CoA. The competitors C_18:1-CoA and MeC₁₈-CoA were added at concentrations of 0.25, 0.5 and 1.0 µM. For each condition, the rate of formation of NBD-PC was calculated from measurements of 3 samples taken between 0 and 6 min. The values obtained in the presence of the competitors are reported as percentages of the values obtained in their absence. Synthesis of odd-chain acyl-CoA was performed twice and were used in several independent competition experiments. The error bars indicate the standard deviation of 3 measurements.