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題 名 | The C-Terminal Segment is Essential for Maintaining the Quaternary Structure and Enzyme Activity of the Nitric Oxide Forming Nitrite Reductase from Achromobacter Cycloclastes |
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作 者 | Chang,Wei-chao; Chen,Jang-yi; Chang,Tschining; Liu,Ming-yih; Payne,William J.; LeGall,Jean; Chang,Wen-chang; | 書刊名 | 中央研究院生物化學研究所論文集 |
卷 期 | 24 1998[民87.] |
頁 次 | 頁23-26 |
分類號 | 361.19 |
關鍵詞 | C-terminal segment; Nitrite reductase; NIR; C-terminal deletion; Nitric oxide forming nitrite reductase; |
語 文 | 英文(English) |
英文摘要 | We have constructed and expressed a series of muteted nitrite reductase (NIR) mutants based on the sequence of NIR from Achromobacter cycloclastes. Deleting a pentapeptide, an undecapeptide, or a heptadecapeptide from the C-terminus of NIR resulted in a series of C-tcrminal deletion mutated proteins designated as NIR-5, NIR-II, and NIR-17, respectively. A C-terminally extended mutated protein, NIR+8, was also produced, which contains an extra octapeptide attached to the C-terminus of the wild-type NIR. An SDS-PAGE system using tris-tricine buffer could retain the native NIR in its trimeric form, thus offering a convenient method to check the quaternary structure of NIR analogs. By using this system it was found that NIR-5 was maintained as trimer and retained 72% of wild-type enzyme activity. However, both NIR-II and NIR-17 behaved as monomers in the SDS-PAGE and lost all their enzyme activity. Although NIR+8 maintained its trimeric structure it was enzymatically inactive. These results clearly indicate that the C-terminal undecapeptide is essential for maintaining the quaternary structure as well as the full en- zymatic activity, as expected from the X-ray crystallography studies. |
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