| 论文题目: | Tailoring Enzymes Involved in the Biosynthesis of Angucyclines Contain Latent Context-Dependent Catalytic Activities |
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| 作者: | Patrikainen, P; Kallio, P; Fan, KQ; Klika, KD; Shaaban, KA; Mantsala, P; Rohr, J; Yang, KQ; Niemi, J; Metsa-Ketela, M |
| 联系作者: | Metsa-Ketela, M |
| 刊物名称: | CHEMISTRY & BIOLOGY |
| 期: | 5 |
| 卷: | 19 |
| 页: | 647-655 |
| 年份: | 2012 |
| 影响因子: | 5.829 |
| 论文下载: | 下载地址 |
| 摘要: | Comparison of homologous angucycline modification enzymes from five closely related Streptomyces pathways (pga, cab, lad, urd, lan) allowed us to deduce the biosynthetic steps responsible for the three alternative outcomes: gaudimycin C, dehydrorabelomycin, and 11-deoxylandomycinone. The C-12b-hydroxylated urdamycin and gaudimycin metabolites appear to be the ancestral representatives from which landomycins and jadomysins have evolved as a result of functional divergence of the ketoreductase LanV and hydroxylase JadH, respectively. Specifically, LanV has acquired affinity for an earlier biosynthetic intermediate resulting in a switch in biosynthetic order and lack of hydroxyls at C-4a and C-12b, whereas in JadH, C-4a/C-12b dehydration has evolved into an independent secondary function replacing C-12b hydroxylation. Importantly, the study reveals that many of the modification enzymes carry several alternative, hidden, or ancestral catalytic functions, which are strictly dependent on the biosynthetic context. |
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