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. 2020 Aug 6;10:13209. doi: 10.1038/s41598-020-70047-5

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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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Kinetic studies of WT PgpB (left panels) and R201A variant (right panels). (A) The C₅₅-PP phosphatase activity was measured as a function of the bulk concentration of substrate but no saturation phenomenon was observed in the range of concentrations that could be tested. (B) The C₅₅-PP phosphatase activity was measured with a fixed concentration of substrate (50 µM) but various concentrations of DDM to reflect the dilution of [¹⁴C]C₅₅-PP at the micellar surface, and the results are expressed as a function of the C₅₅-PP/DDM mole ratio (mol%). The replot of 1/v versus the reciprocal of the C₅₅-PP/DDM mole ratio is also represented.