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. 2020 Jul 21;10:12074. doi: 10.1038/s41598-020-69059-y

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© The Author(s) 2020

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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Effects of FPGS mutation on polyglutamation enzymatic activity using methotrexate as the substrate. (a) FPGS activity was measured by quantifying ATP consumption with a phosphate sensor kit. Wild-type or mutant FPGS proteins were expressed and purified to homogeneity. Mutant FPGS proteins exhibited 30% to 66% reduction in activity under the same experimental conditions. (b) FPGS proteins 2.5 ng (c) FPGS proteins 5.0 ng.