Contribution of conserved Asn residues to the inhibitory activities of kunitz-type protease inhibitors from plants

Shiroh Iwanaga, Nobuyuki Yamasaki, Makoto Kimura, Yoshiaki Kouzuma

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16 Citations (Scopus)

Abstract

Plant Kunitz-type protease inhibitors contain a conserved Asn residue in the N-terminal region. To investigate the role of Asn residue in protease inhibitory activities, Erythrina variegata trypsin inhibitor a (ETIa), E. variegata chymotrypsin inhibitor (ECI), and their mutants, ETIa-N12A and ECI-N13A, were used. Both mutants exhibit weaker inhibitory activities toward their cognate proteases than the wild-type proteins and were readily cleaved at reactive sites. Furthermore, kinetic analysis of the interactions of the mutated proteins with their cognate proteases by surface plasmon resonance (SPR) measurement indicated that replacements of the Asn residue mainly affected dissociation rate constants. The conserved Asn residues of Kunitz-type inhibitors play an important role in exhibiting effective inhibitory activity by stabilizing the structures of the primary binding loop and protease-inhibitor complex.

Original languageEnglish
Pages (from-to)220-223
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume69
Issue number1
DOIs
Publication statusPublished - Jan 2005

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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