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. 2017 Jun 23;7:4160. doi: 10.1038/s41598-017-04539-2

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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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Model of the competitive inhibition of AtSOT18 by PAP. In equilibrium, six different populations of enzyme•ligand complexes are present with their respective probabilities P _ij, where i and j represent the status of the donor and acceptor site, respectively. 0 and 1 represent non-occupied and occupied enzyme sites. ${\tilde{P}}_{i j}$ represents the probability of an enzyme•inhibitor complex species with the inhibitor bound to the donor site. D ₀, A ₀, and I ₀ represent the initial concentration of donor PAPS, acceptor ds-3MTP, and inhibitor PAP, respectively. Dissociation constants are displayed as K _D for the donor, K _A for the acceptor, and K _I for the inhibitor in equilibrium, respectively. The sulfuryl group transfer could only be catalysed within the state P ₁₁ where donor and acceptor site are each occupied with the substrates.