Kinetic Study of the Active Site Structure of β-Amylase from Bacillus cereus var. mycoides

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概要

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• The subsite affinities of the active site of β-amylase from Bacillus cereus var. mycoides were evaluated based on Hiromi's theory, using ^14C-radiolabeled maltooligosaccharides as substrate. It was estimated that the active site consisted of six subsites, and all subsite affinities could be evaluated. The active site had a common subsite arrangement with those of β-amylases from soybean and wheat bran. The intrinsic breakdown rate constant of α-1,4 glucosidic linkage (k_<int>) was five to seven times as large as those of the other enzymes. From the pH dependence of log[k_o/K_m], pK values of two functional ionizable groups were pK_1=4.0 and pK_2=8.4. The pK values were 0.5-0.6 units for pK_1 and 0.2-0.3 units for pK_2 larger than those of the other enzymes. For the affinity-labeling of this enzyme by 2,3 epoxypropyl α-D-glucopyranoside (α-EPG), the binding affinity of α-EPG was 1-1.6 kcal/mol larger than those of the other β-amylases.

• 社団法人日本農芸化学会の論文
• 1996-05-23

著者

• Takasaki Yoshiyuki

  Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University:dainippon Phe

• NITTA Yasunori

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

• Nitta Y

  College Of Agriculture Osaka Prefecture University

• SHIRAKAWA Mayumi

  Department of Materials Science, Faculty of Engineering, Miyazaki University

• Nitta Yasunori

  Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University

• Shirakawa Mayumi

  Department Of Materials Science Faculty Of Engineering Miyazaki University

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