頁籤選單縮合
題 名 | Kinetic Studies of the Inhibitory Effects of Propeptides Subtilisin BPN' and Carlsberg to Bacterial Serine Proteases |
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作 者 | Huang,Hsiau-wen; Chen,Wei-chuan; Wu,Chi-yue; Yu,Hsien-cheng; Lin,Wann-yin; Chen,Shui-tein; Wang,Kung-tsung; | 書刊名 | 中央研究院生物化學研究所論文集 |
卷 期 | 23 1997[民86.] |
頁 次 | 頁227-233 |
分類號 | 361.4 |
關鍵詞 | Propeptide; Serine Protease; Slow binding; Subtilisin BPN'; Subtilisin Carlsberg; |
語 文 | 英文(English) |
英文摘要 | The propeptides of bacterial subtilishin BPN' and Carlsberg were synthesized to investigate their inhibitory function on the enzymes. Kinetically, pro-BPN' inhibits the proteolytic activities of subtilisin BPN□ and Carlsberg separately in a slow binding mode. Pro-Carlsberg behaves as a typical rapid equilibrium competitive inhibitor for these two proteases. Functionally, pro-Carlsberg inhibits the subtilishins with moderate selectivity. The inhibition constant K□ of pro-BPN□ is 5.0 Nm, and 6.1 Nm to subtilisin Carlsberg. The on-rate of pro- BPN' to subtilisin BPN' is 5.8×10□M□s□, and the off-rate 2.9×10□s□. Similarly, the on-rate of pro- BPN' to subtilishin Carlsberg is 2.2×10□ M□s□, and the off-rate 1.3×10□s□. On the other hand, the K□ of pro-Carlsberg to subtilisin BPN' gives 1.3×10□ nM, and 88 nM to subtilisin Carlsberg. Based on the key features of the interactions between pro- BPN' and subtilisin from X-ray crystallographic results (Gallagher et al., 1995), the correlation between the sequence of subtilisin propeptides and their inhibition abilities on the proteases are compared and discussed. |
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