Mechanism-Based Inactivation of Soybean β-Amylase by 2,3-Epoxypropyl α-D-Glucopyranosidc(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
- 社団法人日本農芸化学会の論文
- 1988-01-23
著者
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Isoda Yukihiro
Laboratory Of Biophysical Chemistry College Of Agriculture University Of Osaka Prefecture
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NITTA Yasunori
Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
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Nitta Yasunori
Laboratory Of Biophysical Chemistry College Of Agriculture University Of Osaka Prefecture
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Nitta Yasunori
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
関連論文
- Property of Taka-amylase A with Glu or Asp of the Catalytic Residue Replaced by the Corresponding Amine
- Crystal Structures of β-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents
- Cloning, Sequencing, and Expression of a β-Amylase Gene from Bacillus cereus var. mycoides and Characterization of Its Products
- Kinetic Study of the Active Site Structure of β-Amylase from Bacillus cereus var. mycoides
- Mechanism-Based Inactivation of Soybean β-Amylase by 2,3-Epoxypropyl α-D-Glucopyranosidc(Biological Chemistry)
- Kinetic Study on Maltal Binding Site of Sweet Potato P-Amylase
- Crystal Structure of β-Amylase from Bacillus cereus var. mycoides at 2.2A Resolution
- Attempt at Affinity Labeling of α- and β-Amylases by α- and β-D-Glucopyranosides and α- and β-Maltooligosaccharides with 2,3-Epoxypropyl Residue as Aglycone: Specific Inactivation of β-Amylases(Biological Chemistry)
- Maltal Binding Mechanism and a Role of the Mobile Loop of Soybean β-Amylase
- Two Additional Carbohydrate-Binding Sites of β-Amylase from Bacillus cereus var. mycoides Are Involved in Hydrolysis and Raw Starch-Binding
- Catalytic Mechanism of β-Amylase from Bacillus cereus var. mycoides : Chemical Rescue of Hydrolytic Activity for a Catalytic Site Mutant Glu367→Ala) by Azide
- Crystal Structures of β-Amylase from Bacillus cereus var. mycoides in Complexes with Substrate Analogs and Affinity-Labeling Reagents