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

Shiroh Iwanaga, Nobuyuki Yamasaki, Makoto Kimura, Yoshiaki Kouzuma

研究成果: ジャーナルへの寄稿学術誌査読

16 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)220-223
ページ数4
ジャーナルBioscience, Biotechnology and Biochemistry
69
1
DOI
出版ステータス出版済み - 1月 2005

!!!All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学

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