Substrate specificity determination of mouse implantation serine proteinase and human kallikrein-related peptidase 6 by phage display |
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Authors: | Sharma Navneet Oikonomopoulou Katerina Ito Kenichi Renaux Bernard Diamandis Eleftherios P Hollenberg Morley D Rancourt Derrick E |
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Institution: | Department of Biochemistry and Molecular Biology, University of Calgary, Calgary T2N 4N1, Canada. |
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Abstract: | We constructed a random library of hexapeptides displayed on the surface of bacteriophage T7 to determine the substrate specificity of proteinases. The phage-displayed library was subjected to repeated rounds of biopanning with native implantation serine proteinase and recombinant human kallikrein-related peptidase 6 (KLK6) followed by selection and identification of putative substrates. For both enzymes, the results obtained demonstrate a preference for arginine and lysine at multiple positions in the recognition cleavage motif, confirming their previously reported trypsin-like substrate specificity. In the case of KLK6, there is also a pronounced presence of tryptophan within the cleaved peptide sequences, indicating its potential dual substrate specificity, acting as both a trypsin and chymotrypsin-like enzyme. |
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