Interaction of Subtilisin BPN′ and Recombinant Fungal Protease Inhibitor F from Silkworm with Substituted P₁ Site Residues

Mai TANIGUCHIDepartment of Applied Biology, Kyoto Institute of Technology

Panida ATIWETINDepartment of Applied Biology, Kyoto Institute of Technology

Tomoya HIRAIDepartment of Applied Biology, Kyoto Institute of Technology

Masanobu ITOHDepartment of Applied Biology, Kyoto Institute of Technology

Shigeharu HARADADepartment of Applied Biology, Kyoto Institute of Technology

Saburo HARADepartment of Applied Biology, Kyoto Institute of Technology

Kaeko KAMEIDepartment of Applied Biology, Kyoto Institute of Technology

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Abstract

Fungal protease inhibitor F (FPI-F) from silkworm inhibits subtilisin and fungal proteases. FPI-F mutants P₁ residues of which, Thr²⁹, were replaced with Glu, Phe, Gly, Leu, Met, and Arg, were prepared. The inhibitory activities of mutated FPI-F against subtilisin and other mammalian proteases indicated that FPI-F might be a specific inhibitor toward subtilisin-type protease.

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Interaction of Subtilisin BPN′ and Recombinant Fungal Protease Inhibitor F from Silkworm with Substituted P₁ Site Residues

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Interaction of Subtilisin BPN′ and Recombinant Fungal Protease Inhibitor F from Silkworm with Substituted P1 Site Residues

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Interaction of Subtilisin BPN′ and Recombinant Fungal Protease Inhibitor F from Silkworm with Substituted P₁ Site Residues