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. 2017 Jun 12;8:15758. doi: 10.1038/ncomms15758

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Copyright © 2017, The Author(s)

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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(a) Quantifications of the relative AtACO2 activity treated with different concentrations of POA. Values represent the mean (±s.d.) of three replicates, and the experiment was carried out twice with similar results. (b) Kinetic analysis of AtACO2 inhibition by POA. Activity assays were performed with varying concentration of ACC in the absence and presence of 100, 200 or 300 μM POA. Double-reciprocal plots of initial velocities (Lineweaver–Burk plots) showing a competitive inhibition. The experiment was carried out twice with similar results. (c) Kinetic analysis of the inhibition by POA to AtACO1, AtACO3, AtACO4 and AtACO5. Activity assays were performed with varying concentration of ACC in the absence (+DMSO) and presence of 200 μM POA. The experiment was carried out twice with similar results. (d) The interactions between POA and AtACO2, GA2OX2, ANS as well as DAO were measured using ITC. N.D., not determined.