caa a22 4500 397558341 CHVBK 20180308164809.0 cr unu---uuuuu 161202e199603 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021259 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021259 A New Family of Serine Protease Inhibitors (Bombyx Family) as Established from the Unique Topological Relation between the Positions of Disulfide Bridges and Reactive Site [Elektronische Daten] [Masanobu Itoh, Thitên-Ngoc Pham, Kaeko Hayashi, Ryo Takano, Masaharu Eguchi, Hiroshi Shibata, Takaharu Tanaka, Saburo Hara] The positions of the reactive site and the disulfide bridges in fungal protease inhibitor F (FPI-F) from silkworm (Bombyx mori), which has a unique amino acid sequence and inhibitory specificity, were investigated. At pH 3.0, subtilisin BPN', which is one of target proteases of this inhibitor, specifically cleaved the peptide bond of the inhibitor at Thr(29)-Val(30). The cleaved bond was regenerated by subtilisin BPN' at pH 8.0. These results indicate that the Thr(29)-Val(30) bond of the inhibitor is the reactive site. The locations of disulfide bridges were determined to be Cys(3)-Cys(35), Cys(14)-Cys(27), Cys(18)-Cys(55), and Cy8(37)-Cys(49). Based on the positions of the reactive site and the disulfide bridges, FPI-F is considered to be a member of a new family of serine protease inhibitors. We propose the designation Bombyx family for the new inhibitor family of which FPI-F is a member. © by the Journal of Biochemistry Regular Papers nationallicence Bombyx family inhibitor nationallicence Bombyx mori nationallicence disulfide bridge nationallicence fungal protease inhibitor nationallicence reactive site nationallicence Itoh Masanobu Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto 606 aut Pham Thitên-Ngoc Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut Hayashi Kaeko Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut Takano Ryo Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut Eguchi Masaharu Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto 606 aut Shibata Hiroshi lnstitute for Biomedical Research, Suntory Limited Shimamoto-cho, Mishima-gun, Osaka 618 aut Tanaka Takaharu lnstitute for Biomedical Research, Suntory Limited Shimamoto-cho, Mishima-gun, Osaka 618 aut Hara Saburo Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut The Journal of Biochemistry Oxford University Press 119/3(1996-03), 428-434 0021-924X 119:3<428 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021259 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021259 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Itoh Masanobu Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Pham Thitên-Ngoc Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Hayashi Kaeko Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Takano Ryo Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Eguchi Masaharu Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 700 1- Shibata Hiroshi lnstitute for Biomedical Research, Suntory Limited Shimamoto-cho, Mishima-gun, Osaka 618 aut NATIONALLICENCE 700 1- Tanaka Takaharu lnstitute for Biomedical Research, Suntory Limited Shimamoto-cho, Mishima-gun, Osaka 618 aut NATIONALLICENCE 700 1- Hara Saburo Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology Matsugasaki, Sakyo-ku, Kyoto 606 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/3(1996-03), 428-434 0021-924X 119:3<428 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford