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2003 Fiscal Year Final Research Report Summary

The Metal Binding Motif of Dipeptidyl Peptidase III Influences the Enzyme Act ivity in the Copper Derivative of Dipeptidyl Peptidase III.

Research Project

Project/Area Number 14572042
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Physical pharmacy
Research InstitutionFukuyama University, Department of Applied Biological Science

Principal Investigator

HIROSE Junzo  Fukuyama Univ., Applied Biological Science, Professor, 生命工学部, 教授 (70080215)

Co-Investigator(Kenkyū-buntansha) FUKASAWA Kayoko  Matumoto Dental Univ., 歯学部, 助教授 (60064698)
IWAMOTO Hiroyuki  Fukuyama Univ., Applied Biologocal Science, 助教授 (90213321)
Project Period (FY) 2002 – 2003
Keywordszinc peptidase / zinc binding motif / dipeptidyl peptidase
Research Abstract

The zinc, binding motif (HELLGH) of dipeptidyl peptidase III (DPP III) is different from the common zinc binding motif (HExxH) of metallopeptidases. To clarify the importance of the zinc binding motif part (HELLGH) of DPP III for the enzyme activity, we measured the recovery of the enzyme activity of apo-Leu^<453> dipeptidyl peptidase III (apo-Leu^<453>-del-DPP III), which has a motif (HELGH) like that of the common peptidase (HExxH), in the presence of various metal ions. The enzyme activity of apo-Leu~<453> DPP III could not be recovered by the addition of cupric ions, while apo-DPP III could be easily reactivated by the addition of cupric ions. The visible and EPR spectra of the isolated Cu(II)-Leu^<453>-del DPP III clearly show that the cupric ions of Cu(II)-Leu^<453>-del-DPP III bound to the motif part (HELGH) but didn't exhibit any enzyme activity. The motif part of DPP III directly influences the expression of the enzyme activity in the copper derivative of DPP III. The competitive inhibitor that is not at all digested by DPP III, Hisprophen (His-Pro-Phe-His-Leu-d-Leu-Val-Tyr), have been found out. The inhibition constant (Ki) of Hisprophen for DPP III or Cu(II)-DPP III was 4. 1x10^<-5> 3.8xlO^<-5> M^<-1>, respectively. In the presence of the competitive peptide inhibitor, Hisprophen, the electron paramagnetic resonance (EPR) spectra of Cu(II)-DPP III were completely different from that of Cu(II)-DPP III itself. This result clearly indicates that the metal ions of DPP III locate in the active site and directly interact with the substrate.

  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] K.Tsukahara, J.Hirose et al.: "Intramolecular electron-transfer pathway for deoxy and zinc myoglobins modified with N, N, N', N", N"-diethylenetriaminepentaacetatocobaltate(III)"Bulletin of the Chemical Society of Japan. 76. 2135-2142 (2003)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] 廣瀬順造: "亜鉛ペプチダーゼ中の亜鉛イオンの性質-アミノペプチダーゼ、ジペプチジルペプチダーゼIIIを例として-"福山大学生命工学部年報. 2. 9-16 (2003)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] K.Tsukahara, M.Nishimine, Y., Shioyama, H.Takashima, J.Hirose: "Intramolecular electron-transfer pathway for deoxy and zinc myoglobins modified with N, N, N', N", N"-diethylenetriamine -pentaacetatocobaltate (III)"Bulletin of the Chemical Society of Japan. 76. 2135-2142 (2003)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] J.Hirose: "Characterization of the zinc ions in zinc-peptidases. The examples of Aminopeptidase B and Dipeptidyl Peptidase III"Annual Report of Faculty of Life Science and Biotechnology. 2. 9-16 (2003)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2005-04-19  

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