Increase in Activity for the C-Terminal Pro-X Bond by Site-directed Mutagenesis of Gly137 to Ala in Carboxypeptidase Z
スポンサーリンク
概要
- 論文の詳細を見る
A mutant carboxypeptidase Z from Absidia zychae in which Gly137 was replaced by Ala by site-directed mutagenesis was constructed and expressed in Saccharomyces cerevisiae YPH250. The mutant enzyme hydrolyzed C-tetminal Pro-X bonds (X=amino acid) more efficiently than the wild-type enzyme and sequentially released amino acids from the C-termini of oligopeptides.
- 社団法人日本農芸化学会の論文
- 1996-03-23
著者
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Lee B
National Research Institute Of Brewing
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Ratanakhanokchai Khanok
Laboratory Of Molecular Biology And Microbial Chemistry Tokyo University Of Agriculture And Technolo
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Lee B
Laboratory Of Molecular Biology And Microbial Chemistry Tokyo University Of Agriculture And Technolo
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Kobayashi Yasuo
Laboratory of Molecular Biology and Microbial Chemistry, Tokyo University of Agriculture and Technol
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Takeuchi Michio
Laboratory Enzymology And Microbial Chemistry Tokyo University Of Agriculture And Technology
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Takeuchi Michio
Laboratory Of Molecular Biology And Microbial Chemistry Tokyo University Of Agriculture And Technolo
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LEE Byung
Laboratory of Molecular Biology and Microbial Chemistry, Tokyo University of Agriculture and Technol
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Kobayashi Yasuo
Laboratory Of Molecular Biology And Microbial Chemistry Tokyo University Of Agriculture And Technolo
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Kobayashi Yasuo
Laboratory Of Molecular Biology And Microbial Chemistry Tokyo University Of Agriculture And Technolo
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Lee Byung
Laboratory for Quantum Optics, KAERI, Daejeon 705-353, Republic of Korea
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