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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-269 |
| Subject |
Binding Properties of the N-Terminal and the C-Terminal Domain of Riboflavin Synthase |
| Authors |
Yeohun Hyun, SunJoo Lim, Chan Yong Lee*
Department of Biochemistry, Chungnam National University, Korea
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| Abstract |
To study the biochemical characteristics of RibE from Photobacterium leiognathi, the recombinant plasmids of pQE containing the truncated genes coding for the half of N-terminal and the C-terminal of RibE, as well the whole RibE have been constructed, respectively. The RibE has the amino acid homology with riboflavin synthase from Escherichia coli. Riboflavin synthase catalyzes the formation of one molecule of each riboflavin and 5-amino-6-ribitylamino-2,4-pyrimidinedione from two molecules of 6,7-dimetyl-8-ribityllumazine. Riboflavin synthase from Escherichia coli was shown to be a homotrimer of 23.4 kDa. The most remarkable feature is the intra-molecular sequences similarity between the N-terminal and the C-terminal half of riboflavin synthase from Escherichia coli. Similarly, the proteins have amino acid identity between the N-terminal and the C-terminal domain halves of RibE from Photobacterium leiognathi. The truncated 6X-His tagged proteins of the N-terminal and the C-terminal domain, as well as the whole RibE were purified by binding Ni-column followed by elution with imidazole. The binding properties of the truncated proteins as well as the whole RibE were examined by absorbance and fluorescence spectroscopic analysis with 6,7-dimetyl-8-ribityllumazine and riboflavin. This work was supported by IPET (313058051 HD020). |
| E-mail |
kiddy59@naver.com |
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120th General Meeting of the KCS