マルトビオノラクトンによる大豆β-アミラーゼ水解反応の阻害

• 河野 素子

  Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University

• 新田 康則

  Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University

書誌事項

タイトル別名

• Inhibition of Soybean β-Amylase-Catalyzed Hydrolysis with Maltobionolactone
• Inhibition of Soybean ベータ Amylase Catal

抄録

The reversible conversion between maltobionolactone and maltobionic acid was analyzed kinetically; the rate constants were determined at each pH, and the pKa of maltobionic acid was estimated to be 3.60±0.02. The inhibition by maltobionolactone for the hydrolysis of soluble starch was inves tigated at pH 5.4 and 25t, and it was found that maltobionolactone was a competitive inhibitor with a K₁ of 0.40 mNi. The unitary binding affinity (7.0 kcal?mol^-1) was the same as that of maltotetraose (a substrate). From the result, taking the subsite affinities of this enzyme into account, it was presumed that maltobionolactone consisting of a gluconolactone, with half-chair or sofa conformation, and a glucose (Cl form) is a transition state analogue and binds at subsites 1 and 2.

収録刊行物

• 応用糖質科学

  応用糖質科学 43 (2), 161-165, 1996

  日本応用糖質科学会

詳細情報

• CRID: 1390001205171803648
• NII論文ID: 10008255305
• NII書誌ID: AN10453916
• DOI: 10.11541/jag1994.43.161
• COI: 1:CAS:528:DyaK28XkvVGnu7s%3D
• ISSN: 18844898
• ISSN: 13403494
• NDL書誌ID: 3995010
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I3995010
• データソース種別:
  • JaLC
  • NDL
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可