Subsite structure and action mode of the .ALPHA.-amylase from Thermoactinomyces vulgaris.

• SANO Mutsumi

  Department of Agricutural Chemistry, Faculty of Agriculture, Tokyo Noko University Present address: Central Research Laboratory, Takara Shuzo Co., Ltd.

• SAKANO Yoshiyuki

  Department of Agricutural Chemistry, Faculty of Agriculture, Tokyo Noko University

• KOBAYASHI Tsuneo

  Department of Agricutural Chemistry, Faculty of Agriculture, Tokyo Noko University

抄録

The subsite structure of Thermoactinomyces vulgaris α-amylase was estimated from its action mode and rate parameters of hydrolysis on maltooligosaccharides. These results led to the conclusion that this α-amylase has six subsites with the catalytic site located between the third and fourth subsites from the non-reducing end side. Subsite affinities were calculated to be 0.38, 5.46, 2.72 and 0.23 kcal/mol for subsites 1, 2, 5 and 6, respectively, and the sum of the affinities of subsite 3 and 4 to be - 3.41 kcal/mol. The unique action mode of this α-amylase on various substrates was interpreted in terms of the subsite structure.

収録刊行物

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 49 (10), 2843-2846, 1985

  公益社団法人 日本農芸化学会

キーワード

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

詳細情報

• CRID: 1390282681440938240
• NII論文ID: 130000026607
• DOI: 10.1271/bbb1961.49.2843
• COI: 1:CAS:528:DyaL2MXmtV2rtL4%3D
• ISSN: 18811280
• ISSN: 00021369
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可