Subsite structure of Saccharomycopsis .ALPHA.-amylase secreted from Saccharomyces cerevisiae.
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概要
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The kinetic parameters (kcat/Km) and the cleaved-bond distributions for the hydrolysis of linear maltooligosaccharides Gn (3_??_n_??_9) by Saccharomycopsis α-amylase (Sfamy) secreted from Saccharomyces cerevisiae were determined at pH 5.25 and 25°C. The subsite affinities of Sfamy were also evaluated from these data. The subsite structure of Sfamy is characteristic of the active site of an endo-cleavage type enzyme, consisting of internal repulsive sites with the catalytic residues and external attractive sites. Moreover, the pKa values of the catalytic residues were calculated from the pH dependence plot of the kinetic parameter (kcat/Km). The amino acid residues which contribute to the subsite affinities and the catalytic activity of Sfamy are proposed and compared with those of Taka-amylase A.
- 社団法人 日本生化学会の論文
著者
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Matsui Eriko
National Institute of Bioscience and Human-Technology
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Fukui Sakuzo
Department Of Bioengineering Faculty Of Engineering Fukuyama University
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Miyairi Sachio
National Chemical Laboratory for Industry
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HONDA Koichi
National Chemical Laboratory for Industry
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Ishikawa Kazuhiko
National Chemical Laboratory For Industry
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Matsui Ikuo
National Chemical Laboratory for Industry
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