Substrate Specificity of a Novel Alcohol Resistant Metalloproteinase, Vimelysin, from Vibrio sp. T1800
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概要
- 論文の詳細を見る
Vimelysin is a novel alcohol resistant metalloproteinase from Vibrio sp. T1800. The substrate specificity of vimelysin was studied by using natural and furylacryloyl dipeptide substrates. Vimelysin cleaved mainly Pro^7-Phe^8 bond and slightly Tyr^4-Ile^5 bond in human angiotensin I. Vimelysin also cleaved mainly Phe^<24>-Phe^<25> and Tyr^<16>-Leu^<17> bonds, and slightly His^5-Leu^6, His^<10>-Leu^<11>, Ala^<14>-Leu^<15>, and Gly^<23>-Phe^<24> bonds in oxidized insulin B-chain. The substrate specificity of vimelysin, by using furylacryloyl (Fua) dipeptides were also studied. The ratio of k_<cat>/K_m for Fua-Gly-Phe-NH_2/Fua-Gly-Leu-NH_2, Fua-Phe-Leu-NH_2/Fua-Gly-Leu-NH_2, and Fua-Phe-Phe-NH_2/Fua-Gly-Leu-NH_2 were 15.9, 27.8, and 59.0, respectively. These results indicate that vimelysin easily recognizes phenylalanine in P1' positions, which is different from thermolysin.
- 社団法人日本農芸化学会の論文
- 1996-10-23
著者
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ODA Kohei
Department of Applied Biology, Kyoto Institute of Technology
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Takahashi S
Akita Res. Inst. Food And Brewing Akita
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功刀 滋
京工繊・繊維
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KUNUGI Shigeru
Department of Polymer Science and Engineering, Kyoto Institute of Technology
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TAKAHASHI Saori
Department of Bioengineering, Akita Research Institute of Food and Brewing (ARIF)
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Oda Kohei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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OKAYAMA Kiyoaki
Department of Applied Biology, Faculty of Textile Science, Kyoto Institute of Technology
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Kunugi Shigeru
Department Of Biomolecular Engineering Graduate School Of Science And Technology Kyoto Institute Of
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Oda K
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Suzuki Takahito
Biological Laboratory Faculty Of Science Nara Women's University
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Takahashi Saori
Department Of Applied Biology Faculty Of Textile Science Kyoto Institute Of Technology
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Kunugi Shigeru
Department of Applied Chemistry
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