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)

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概要

• 論文の詳細を見る

• Among 2,3-epoxypropyl α-D-glucopyranoside and 2,3-epoxypropyl α-maltooligosaccharides and the β-anomers, 2,3-epoxypropyl α-D-glucopyranoside (α-EPG) strongly inactivated the β-amylases [EC 3.2.1.2] of sweet potato, barley, and Bacillus cereus, in addition to soybean β -amylase [J. Biochem., 99, 1631 (1986)]. However, none of the compounds used inactivated any α-amylases [EC 3.2. 1.1] of porcine pancreas, Aspergillus oryzae, or Bacillus amyloliquefaciens. Irreversible incorporation of ^<14>C-labeled α-EPG into β-amylases was stoichiometric, i.e., one α-EPG per active site of the enzyme was bound, and the inactivations were almost complete. The results suggest that α-EPG is an affinity labeling reagent selective for β-amylase. Slow inactivations by the other compounds were also observed, depending on the difference of source of β-amylase.

• 社団法人日本農芸化学会の論文
• 1987-12-23

著者

• Isoda Y

  Univ. Osaka Prefecture Sakai Jpn

• Isoda Yukihiro

  Laboratory Of Biophysical Chemistry College Of Agriculture University Of Osaka Prefecture

• Nitta Y

  Univ. Osaka Prefecture Sakai Jpn

• Nitta Yasunori

  Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University

• ASANAMI Shogo

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

• Asanami Shogo

  Laboratory Of Biophysical Chemistry College Of Agriculture University Of Osaka Prefecture

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

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