| 论文题目: | Engineering a Carbohydrate-processing Transglycosidase into Glycosyltransferase for Natural Product Glycodiversification |
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| 作者: | Liang Chaoning, Zhang Yi, Jia Yan, Wang Wenzhao, Li Youhai, Lu Shikun, Jin Jian-Ming*, and Tang Shuang-Yan*. |
| 联系作者: | |
| 刊物名称: | Sci Rep |
| 期: | |
| 卷: | 6 |
| 页: | 21051 |
| 年份: | 2016 |
| 影响因子: | 5.597 |
| 论文下载: | 下载地址 |
| 摘要: | Glycodiversification broadens the scope of natural product-derived drug discovery. The acceptor substrate promiscuity of glucosyltransferase-D (GTF-D), a carbohydrate-processing enzyme from Streptococcus mutans, was expanded by protein engineering. Mutants in a site-saturation mutagenesis library were screened on the fluorescent substrate 4-methylumbelliferone to identify derivatives with improved transglycosylation efficiency. In comparison to the wild-type GTF-D enzyme, mutant M4 exhibited increased transglycosylation capabilities on flavonoid substrates including catechin, genistein, daidzein and silybin, using the glucosyl donor sucrose. This study demonstrated the feasibility of developing natural product glycosyltransferases by engineering transglycosidases that use donor substrates cheaper than NDP-sugars, and gave rise to a series of alpha-glucosylated natural products that are novel to the natural product reservoir. The solubility of the alpha-glucoside of genistein and the anti-oxidant capability of the alpha-glucoside of catechin were also studied. |
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