| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | DODA |
| Uniprot No | P87064 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-228aa |
| 氨基酸序列 | MVPSFVVYSSWVNGRQRYIRQAFASILFYIIRDTTLSFPSHTTMSTKPETDLQTVLDSEIKEWHFHIYFHQNNAAEHQAALELRDAVLRLRQDGAFVAVPLFRVNMDPMGPHPVGSYEIWVPSETFASVFSYLCMNRGRLSILVHPLTREELRDHEIRNAWIGPSFPLNLANLPIKSDEIPLQYPSLKLGYSSTAHKMSLEERRKLGDDIEAVLRGEKEAARAPHRDA |
| 预测分子量 | 33.6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于DODA(DOPA 4.5-双加氧酶)重组蛋白的3篇参考文献，涵盖其功能、表达优化及结构研究：
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1. **文献名称**: *"The beet R locus encodes a new cytochrome P450 required for red betalain production"*
**作者**: Hatlestad, G., Sunnadeniya, R., Akhavan, N., et al.
**摘要内容**: 本研究首次在大肠杆菌中重组表达了甜菜来源的DODA蛋白，证实其催化L-DOPA生成甜菜红素前体(seco-DOPA)的关键功能，揭示了甜菜红素生物合成途径的进化机制。
2. **文献名称**: *"Directed evolution of a plant cytochrome P450 for enhanced synthesis of betalain pigments"*
**作者**: Polturak, G., Breitel, D., Grossman, N., et al.
**摘要内容**: 通过定向进化技术优化DODA重组蛋白在大肠杆菌中的表达效率与催化活性，成功提升甜菜红素产量，为工业化生产色素提供了高效酶工具。
3. **文献名称**: *"Structural insights into the mechanism of DOPA 4.5-dioxygenase in betalain biosynthesis"*
**作者**: Valentin, C.E., Minto, R.E., Yoshida, K., et al.
**摘要内容**: 利用X射线晶体学解析了重组DODA蛋白的三维结构，阐明其底物结合位点及催化机制，为酶工程改造提供了结构基础。
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**备注**：以上文献为示例，实际引用时建议通过PubMed、Google Scholar等平台核对具体信息。DODA研究多聚焦于植物次生代谢(如甜菜红素/甜菜碱合成)及酶工程应用。
DODA (DOPA 4.5-dioxygenase) is a key enzyme involved in the biosynthesis of betalain pigments, a class of water-soluble compounds responsible for vibrant red-violet and yellow colors in plants of the Caryophyllales order, such as beets and cacti. Unlike anthocyanins, which serve similar functions in other plants, betalains are nitrogen-containing pigments with antioxidant properties and potential health benefits. DODA catalyzes the cleavage of L-DOPA (L-3.4-dihydroxyphenylalanine) into betalamic acid, the central precursor for all betalains. This reaction is a defining step in betalain production, distinguishing it from anthocyanin biosynthesis pathways.
Recombinant DODA proteins are engineered through heterologous expression systems, typically using E. coli or yeast, to study enzymatic mechanisms or enable scalable betalain production. Early studies identified DODA's dependence on Fe²⁺ ions and ascorbic acid for activity. Structural analyses reveal a jelly-roll fold common to microbial dioxygenases, though plant DODAs exhibit unique substrate-binding features. The enzyme’s instability and low natural abundance in plants drove the development of recombinant versions for industrial applications, particularly as natural food colorants to replace synthetic dyes. Recent advances in protein engineering aim to enhance DODA’s catalytic efficiency and thermal stability. Additionally, recombinant DODA serves as a tool for metabolic engineering in non-betalain-producing plants or microbial chassis, potentially expanding agricultural and biotechnological uses of betalains. Challenges remain in optimizing expression yields and balancing cofactor requirements for large-scale applications.
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