Purification of an Aminopeptidase Preferentially Releasing N-terminal Alanine from Cucumber Leaves and Its Identification as a Plant Aminopeptidase N.

• YAMAUCHI Yasuo

  Faculty of Agriculture, Tottori University

• EJIRI Yukinori

  Faculty of Agriculture, Tottori University

• TANAKA Kiyoshi

  Faculty of Agriculture, Tottori University

抄録

In this study, a highly active foliar aminopeptidase preferentially releasing N-terminal alanine from artificial substrates was purified and characterized from cucumber (Cucumis sativus L. suyo). The enzyme had a molecular mass of 200 kDa consisting of two subunits of 95 kDa. It was a metalloprotease the pH optimum of which was 8 to 9. It cleaved Ala-, Gly-, Met-, Ser-, Leu-, Lys-, and Arg artificial substrates. An internal amino acid sequence was similar to those of aminopeptidase N (clan MA, family M1) of microorganisms, and was very similar to that of a putative aminopeptidase N of Arabidopsis thaliana. From these results, the highly active aminopeptidase in cucumber leaves was identified to be a plant aminopepitdase N.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 65 (12), 2802-2805, 2001

  公益社団法人 日本農芸化学会

キーワード

• Cucumis sativus
• cucumber
• purification
• aminopeptidase N
• naphthylamidase

詳細情報

• CRID: 1390282681449497600
• NII論文ID: 110002693361
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.65.2802
• COI: 1:CAS:528:DC%2BD38XjtVymsQ%3D%3D
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 6027506
• PubMed: 11826983
• Web Site: http://id.ndl.go.jp/bib/6027506
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6027506
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.65.2802
• 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