Inhibition of Achromobacter Protease I by Lysinal Derivatives
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概要
- 論文の詳細を見る
Z-Val-, Z-Pro-, Z-Leu-Leu-, and Z-Leu-Pro-lysinals and Bz-DL-lysinal were chemically synthesized and tested as novel inhibitors for Achromobacter protease I (API), a lysine-specific serine protease. Among the lysinal derivatives tested, Z-Val-lysinal was the most potent competitive inhibitor, its K_i being estimated as 6.5 nM in an esterolytic assay with Tos-Lys-OMe. In an amidolytic assay, Z-Leu-Leu-lysinal was the most potent inhibitor and the apparent mode of inhibition was non-competitive. The K_is of the other lysinal derivatives in both esterolytic and amidolytic assays were more than 10^3 times lower than that of leupeptin. Z-Val-lysinol, lacking the aldehyde group, was a poor competitive inhibitor. These results suggest that acyl-, aclyaminoacyl-, and acylpeptidyllysinals function as a transition-state inhibitor for Achromobacter protease I.
- 社団法人日本農芸化学会の論文
- 1992-10-23
著者
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Sakiyama F
International Buddhist University
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Sakiyama Fumio
Division Of Protein Chemistry Institute For Protein Research Osaka University
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Sakiyama Fumio
Institute For Protein Research Osaka University
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Masaki Takeharu
Department of Resource Biology, Faculty of Agriculture, Ibaraki University
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Tsunasawa Susumu
Institute for Protein Research, Osaka University
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Soejima Masami
Department of Resource Biology, Faculty of Agriculture, Ibaraki University
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TANAKA Takumi
Osaka Research Laboratories, Wako Pure Chemical Industries, Ltd.
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Soejima Masami
Department Of Resource Biology Faculty Of Agriculture Ibaraki University
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Masaki T
Department Of Bioresource Science College Of Agriculture Ibaraki University
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Masaki Takeharu
Department Of Agricultural Chemistry Faculty Of Agriculture Ibaraki University
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Tanaka Takumi
Osaka Research Laboratories Wako Pure Chemical Industries Ltd.
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Tsunasawa S
Takara Shuzo Co. Ltd. Shiga
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Tsunasawa Susumu
Institute For Protein Research Osaka University
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Soejima Masami
Department Of Agricultural Chemistry Faculty Of Agriculture Ibaraki University
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