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. 2021 Mar 19;12:1728. doi: 10.1038/s41467-021-21924-8

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© The Author(s) 2021

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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Fig. 3 — a Wild type and mutant enzymes were assayed for LTC₄ synthase activity. Error bars represent the mean values ± standard deviations of three to four independent activity measurements. b Thiolate anion formation in MGST2: UV difference spectra recorded from 230 to 285 nm demonstrate the thiolate anion peak at 239 nm, which is absent in Arg104Ala mutant and in the presence of GSO₃⁻ inhibitor. Source data are provided as a Source data file.