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Substrate specificity and physiological function of mammalian dipeptidases

Research Project

Project/Area Number 15K06997
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Research Field Functional biochemistry
Research InstitutionOsaka University

Principal Investigator

Okumura Nobuaki  大阪大学, たんぱく質研究所, 准教授 (20224173)

Project Period (FY) 2015-04-01 – 2018-03-31
Project Status Completed (Fiscal Year 2017)
Budget Amount *help
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Keywordsジペプチド / カルノシン / ヒスチジン / βアラニン / 金属プロテアーゼ / タンパク質代謝 / ペプチダーゼ / 酵素反応 / ジペプチダーゼ / 基質特異性 / 蛋白質代謝 / ペプチド代謝 / イミダゾールジペプチド
Outline of Final Research Achievements

Dipeptides are produced and degraded in mammalian cells during protein turnover and digestion to obtain amino acids required for nutritional demands. In addition, some kinds of dipeptides such as carnosine are synthesized from amino acids in specific organs and play some specific roles as a bioactive molecule. We have previously found that a metallopeptidase CN2 hydrolyses several kinds of dipeptides including carnosine. In this study, we have determined the substrate specificity of CN2, and shown that CN2-Mn2+ and CN2-Zn2+ complexes have different substrate specificity. When substrate specificity in cultured cells was examined, it was more similar to that of the CN2-Zn2+ complex observed in in vitro enzyme assay. These results demonstrate the role of CN2 in the final step of protein and peptide breakdown.

Report

(4 results)
  • 2017 Annual Research Report   Final Research Report ( PDF )
  • 2016 Research-status Report
  • 2015 Research-status Report
  • Research Products

    (4 results)

All 2017 2016 Other

All Journal Article (2 results) (of which Peer Reviewed: 2 results,  Acknowledgement Compliant: 1 results) Presentation (1 results) Remarks (1 results)

  • [Journal Article] The zinc form of carnosine dipeptidase 2 (CN2) has dipeptidase activity but its substrate specificity is different from that of the manganese form2017

    • Author(s)
      Okumura T. and Takao T
    • Journal Title

      Biochem Biophys Res Commun.

      Volume: 494 Issue: 3-4 Pages: 484-490

    • DOI

      10.1016/j.bbrc.2017.10.100

    • Related Report
      2017 Annual Research Report
    • Peer Reviewed
  • [Journal Article] Evidence for an essential role of intradimer interaction in catalytic function of carnosine dipeptidase II using electrospray-ionization mass spectrometry.2016

    • Author(s)
      Okumura N, Tamura J, Takao T.
    • Journal Title

      Protein Science

      Volume: 25 Issue: 2 Pages: 511-522

    • DOI

      10.1002/pro.2842

    • Related Report
      2015 Research-status Report
    • Peer Reviewed / Acknowledgement Compliant
  • [Presentation] カルノシンジペプチダーゼ2(CN2) に結合する金属イオンと基質特異性の解析2017

    • Author(s)
      奥村宣明
    • Organizer
      2017年度生命科学系学会合同年次大会(第90回日本生化学会大会)
    • Related Report
      2017 Annual Research Report
  • [Remarks] 体内環境統合蛋白質研究グループ

    • URL

      http://www.protein.osaka-u.ac.jp/metabolism/taisha.html

    • Related Report
      2016 Research-status Report

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Published: 2015-04-16   Modified: 2019-03-29  

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