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. 2019 Oct 31;9:15725. doi: 10.1038/s41598-019-51749-x

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© The Author(s) 2019

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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Mutation of the catalytic histidine residue at position 125 affects glucosinolate sulfatase (GSS) activity of PcGSS2. PcGSS2 and PcGSS2 H125N were heterologously expressed in High Five^TM insect cells and incubated with eight different glucosinolate substrates for 2 h at 35 °C. Extracted LC-MS/MS ion chromatograms of desulfo-indol-3-ylmethyl glucosinolate (I3M glucosinolate) are shown. Remaining I3M glucosinolate in the assay was detected as desulfo-I3M glucosinolate due to in-source fragmentation in positive ionization mode.