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. 2020 Jul 21;10:12117. doi: 10.1038/s41598-020-69079-8

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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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Kinetics and α2-AP inhibition. (a) An example of Michealis–Menten kinetic measurement of wild-type µPlm. (b) Comparison of α2-AP inhibition of wild-type and F587A, shows the reduced inhibition of F587A by α2-AP. (c) Kinetic parameters of loop 2 and 3 alanine mutants, showed the increased catalytic efficiency (Kcat/Km) of F587A. (d) Kinetic parameters and α2-AP inhibition of loops 1–5. Blue bars represent fold of catalytic efficiency, and the red bars represent fold of IC50 relative to the wild-type. (d-1) loop 1; (d-2) loop 2; (d-3) loop 3; (d-4) loops 4 and 5. (e) Same as (d), with loops 6–8 and F587 saturation mutants. (e-1) Loop 6; (e-2) loop 7; (e-3) loop 8; (e-4) F587 saturation mutants, including all 20 amino acid changes.