Effects of Dimethyl Sulfoxide, Temperature, and Sodium Chloride on the Activity of Human Matrix Metalloproteinase 7 (Matrilysin).

• Oneda Hiroshi

  Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

• Inouye Kuniyo

  Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

抄録

Effects of dimethyl sulfoxide (DMSO), temperature, and sodium chloride on the matril-ysin-catalyzed hydrolysis of (7-methoxycoumarin-4-yl) acetyl-L-Pro-L-Leu-Gly-L-Leu-[N³-(2, 4-dinitrophenyl)-L-2, 3-diamino-propionyl]-L-Ala-L-Arg-NH₂ [MOCAc-PLGL (Dpa) AR] were examined. DMSO inhibited the matrilysin activity competitively with the inhibitor constant (K_i) of 0.59±0.04 M, and the binding between them was endothermic and entropy-driven. The binding of matrilysin with MOCAc-PLGL (Dpa) AR was also found to be entropy-driven. The matrilysin activity was increased in a biphasic exponential fashion with increasing concentration of NaCl, and was 5.3 times higher in the presence of 4M NaCl than that in its absence. The first and second phases were separated at 0.5M NaCl, and the activation at x M NaCl compared with the activity in the absence of NaCl was expressed as 2.1^x at [NaCl]<0.5M and 1.4^x at [NaCl]>0.5M. The activation was brought about solely through a decrease in the Michaelis constant (K_m), and the cata-lytic constant (k_cat) was not much altered. This suggests that the decrease in the electro-static interaction and the increase in the hydrophobic interaction between matrilysin and the substrate might enhance the enzyme activity by reducing the K_m value.

収録刊行物

• The Journal of Biochemistry

  The Journal of Biochemistry 128 (5), 785-791, 2000

  社団法人 日本生化学会

キーワード

• dimethyl sulfoxide
• enzyme activity
• matrilysin
• matrix metalloproteinase
• salt activation
• temperature

詳細情報

• CRID: 1390282679908522880
• NII論文ID: 130003534008
• NII論文ID: 10005834479
• NII書誌ID: AA00694073
• DOI: 10.1093/oxfordjournals.jbchem.a022816
• COI: 1:CAS:528:DC%2BD3MXpsFSn
• ISSN: 17562651
• ISSN: 0021924X
• ISSN: http://id.crossref.org/issn/0021924X
• NDL書誌ID: 5557239
• PubMed: 11056391
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5557239
• Web Site: http://academic.oup.com/jb/article-pdf/128/5/785/2477027/128-5-785.pdf
• Web Site: https://search.jamas.or.jp/link/ui/2001141806
• 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