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. 2017 Jul 28;7:6789. doi: 10.1038/s41598-017-06680-4

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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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KLK7 and mKLK7 protein identity. (a) Surface exposed residues corresponding to the catalytic triad (His57, Asp102 and Ser195; Schechter and Berger notation¹²) of KLK7 were identified on the three dimensional (3D) structure available in Protein Data Bank (PDB, accession: 2QXG.pdb in standard serine protease orientation) using SPDBV v4.10. (b) In addition, S195A mutation was made using the mutation tool on SPDBV v4.10. Alongside, are the peptides identified in the MS analysis (Underlined; identified with a 99% protein probability and 95% peptide probability cut off) of trypsin-digested (a) active KLK7 and (b) mKLK7 aligned with the KLK7 full length protein (UniProtKB; P49862-1). The pro-signal peptide (in blue box) was not included in the expression construct, thus obtaining mature amino acid sequences for these peptidases. Expected mutation, S195A was identified in the MS-identified mKLK7 peptide sequence as highlighted in red bold letter.