| Autor: |
Morita, Masatomo, Tanji, Yasunori, Orito, Yuji, Mizoguchi, Katsunori, Soejima, Aya, Unno, Hajime |
| Zdroj: |
FEBS Letters; June 2001, Vol. 500 Issue: 1-2 p56-59, 4p |
| Abstrakt: |
To analyze the antibacterial activity of Bacillus amyloliquefaciensphage endolysin, nine deletion derivatives of the endolysin were constructed. Each deletion mutant was overexpressed, purified and characterized. The catalytic domain was located on the N‐terminal region and the C‐terminus had an affinity with the bacterial envelope. The enzymatic activity remained in spite of the deletion of the C‐terminal 116‐amino acid region; however, the antibacterial activity was lost. These results indicate that antibacterial action requires both the C‐terminal cell‐binding and the N‐terminal enzymatic activities. |
| Databáze: |
Supplemental Index |
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