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. 2017 Sep 21;16:382. doi: 10.1186/s12936-017-2032-4

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 1 — Kinetic analysis of PfA-M1 inhibition by compound T5. a PfA-M1 activity was measured with increasing Ala-pNA chromogenic substrate concentrations (S1 = Km/2, S2 = Km and S3 = 2 km) over a range of inhibitor concentrations [I], from 0.01 to 0.1 μM. Dixon linearization plots are shown for PfA-M1 enzyme versus T5 or bestatin. b Competitive inhibition was assessed by plotting the slope of the primary Dixon plot versus the inverse of the substrate concentration and was inferred by the straight line passing through the origin. Results are presented as the mean ± SEM from three independent measurements