Subsite Structure and Action Mode of the α-Amylase from Thermoactinomyces vulgaris
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概要
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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.
- 社団法人 日本農芸化学会の論文
著者
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KOBAYASHI TSUNEO
Department of Natural Sciences (Physics), School of Medicine, Fukushima Medical University
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SANO Mutsumi
Department of Agricutural Chemistry, Faculty of Agriculture, Tokyo Noko University
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SAKANO Yoshiyuki
Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University
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SAKANO Yoshiyuki
Department of Agricutural Chemistry, Faculty of Agriculture, Tokyo Noko University
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KOBAYASHI Tsuneo
Department of Agricultural Chemistry, Faculty of Agriculture, Tokyo Noko University
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