Kinetic Study on Maltal Binding Site of Sweet Potato P-Amylase
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概要
- 論文の詳細を見る
Sweet potato β-amylase catalyzes two different kinds of reactions:hydrolysis of amylose, etc. and hydration of maltal (α-D-glucopyranosyl-(1→4)-2-deoxy-D-glucal). To investigate whether both the reactions are catalyzed at the same catalytic site or not, an inhibition study on both the reactions and an affinity-labeling of Glu187 were done using 4-O-α-D-glucopyranosyl-(1→4)-1-deoxy-nojirimycin (GDN) as an inhibitor. As GDN showed competitive inhibition with the same K_i for these reactions, it was concluded that both the reactions occur at the same catalytic site.
- 社団法人日本農芸化学会の論文
- 1996-06-23
著者
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Nakashima Takuji
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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Matsumoto Yasuo
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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NITTA Yasunori
Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
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KOHNO Motoko
Laboratory of Biophysical Chemistry, College of Agriculture, Osaka Prefecture University
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Nitta Yasunori
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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Kohno Motoko
Laboratory Of Biophysical Chemistry College Of Agriculture Osaka Prefecture University
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