Inhibitory Effects of Alcohols on the Activity of Human Matrix Metalloproteinase 7 (Matrilysin)

• MUTA Yuko

  Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• ONEDA Hiroshi

  Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

• INOUYE Kuniyo

  Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

抄録

Aliphatic alcohols inhibited the activity of human matrix metalloproteinase 7 (matrilysin) competitively with K_i of 6.1–19.4% (v/v) or 0.66–4.80 M. From the relationship between the structures of alcohols and their K_i values, alcohols are considered to bind the hydrophobic S1′ subsite most plausibly, and the size of the pocket was estimated to be large enough to accommodate the length of 1-butanol (4-carbon chain) and the bulk of tertiary alcohols. Alcohols might be suitable probes for exploring the active-site geometry of enzymes.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 68 (12), 2649-2652, 2004

  公益社団法人 日本農芸化学会

キーワード

• aliphatic alcohol
• competitive inhibition
• enzyme inhibitor
• matrilysin
• matrix metalloproteinase

詳細情報

• CRID: 1390282681449763072
• NII論文ID: 130000030904
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.68.2649
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 7197569
• PubMed: 15618645
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I7197569
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.68.2649
• Web Site: https://search.jamas.or.jp/link/ui/2006178668
• 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