Some Molecular and Inhibitory Specifications of a Dipeptidyl Carboxypeptidase from the Polychaete Neanthes virens Resembling Angiotensin 1 Converting Enzyme

• KAWAMURA Toshiya

  Industrial Technology Center of Nagasaki

• KIKUNO Kiyofumi

  Division of Biochemistry, Faculty of Fisheries, Nagasaki University

• ODA Tatsuya

  Division of Biochemistry, Faculty of Fisheries, Nagasaki University

• MURAMATSU Tsuyoshi

  Division of Biochemistry, Faculty of Fisheries, Nagasaki University

書誌事項

タイトル別名

• Some Molecular and Inhibitory Specifications of a Dipeptidyl Carboxypeptidase from the Polychaete Neanthes virens Resembling Angiotensin I Converting Enzyme.
• Some Molecular and Inhibitory Specifications of a Dipeptidyl Carboxypeptidase from the Polychaete<i>Neanthes virens</i>Resembling Angiotensin I Converting Enzyme

抄録

  Dipeptidyl carboxypeptidase (DCP) from the polychaete Neanthes virens, resembling mammalian angiotensin I converting enzyme (ACE), was studied to discover some of its molecular and inhibitory properties, as the first evidence of these in a marine invertebrate. Amino acid and carbohydrate contents were analyzed. The N-terminal amino acid sequence of N. virens DCP was (NH₂)D-E-E-A-G-R-Q-W-L-A-E-Y-D-L-R-N-Q-T-V-L-. Peptide maps of N. virens DCP from lysyl endopeptidase digestion were different from rabbit p-ACE. The far-ultraviolet circular dichroic spectra of N. virens DCP indicated that the secondary structure of this enzyme seemed to be an α-helical structure and was similar to that of rabbit p-ACE, but the near-ultraviolet circular dichroic spectra of N. virens DCP indicated that the aromatic amino acid residue circumambience of this enzyme was different from rabbit p-ACE. The effects of several reagents for chemical modification of amino acids on the activity of N. virens DCP were tested. Arg, Tyr, Glu, and/or Asp, His, Trp, and Met caused loss of the activity. In addition, the IC₅₀ and K_i values for a well-known ACE inhibitor, Val-Tyr, which was a competitive inhibitor of N. virens DCP, were 263 and 20 μM, respectively. These results suggested that N. virens DCP is different from mammalian ACE in the molecular and inhibitory properties, although the same substrate specificity was demonstrated in a previous paper.<br>

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 64 (10), 2193-2200, 2000

  公益社団法人 日本農芸化学会

キーワード

• angiotensin I converting enzyme
• dipeptidyl carboxypeptidase
• inhibitory property
• molecular property
• <i>Neanthes virens</i>

詳細情報

• CRID: 1390001206474254720
• NII論文ID: 110002679795
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.64.2193
• COI: 1:CAS:528:DC%2BD3cXnvVOhtLY%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 5558602
• PubMed: 11129594
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5558602
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.64.2193
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可