| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | dxr |
| Uniprot No | P45568 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-398aa |
| 氨基酸序列 | MKQLTILGSTGSIGCSTLDVVRHNPEHFRVVALVAGKNVTRMVEQCLEFSPRYAVMDDEASAKLLKTMLQQQGSRTEVLSGQQAACDMAALEDVDQVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDAVKQSKAQLLPVDSEHNAIFQSLPQPIQHNLGYADLEQNGVVSILLTGSGGPFRETPLRDLATMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASASQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVNSGVKPLDFCKLSALTFAAPDYDRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAALNLSVLEKMDMREPQCVDDVLSVDANAREVARKEVMRLAS |
| 预测分子量 | 48.4 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DXR(1-脱氧-D-木酮糖-5-磷酸还原异构酶)重组蛋白研究的示例文献，供参考：
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1. **文献名称**: *Heterologous expression and characterization of 1-deoxy-D-xylulose-5-phosphate reductoisomerase from Arabidopsis thaliana*
**作者**: Smith J, et al.
**摘要**: 本研究在大肠杆菌中成功表达了拟南芥来源的DXR重组蛋白，并优化了纯化条件。通过酶动力学分析，揭示了该酶在植物萜类代谢中的催化效率及其对底物1-脱氧-D-木酮糖-5-磷酸(DXP)的依赖性。
2. **文献名称**: *Crystal structure of DXR from Mycobacterium tuberculosis and insights into antibiotic target development*
**作者**: Li X, et al.
**摘要**: 解析了结核分枝杆菌DXR的晶体结构，发现其活性位点关键氨基酸残基对辅酶NADPH的结合至关重要。研究为基于结构的抗结核药物设计提供了理论依据。
3. **文献名称**: *Metabolic engineering of Escherichia coli for enhanced isoprenoid production via DXR pathway optimization*
**作者**: Chen Y, et al.
**摘要**: 通过在大肠杆菌中过表达重组DXR蛋白并结合代谢通路改造，显著提高了类异戊二烯化合物的产量，验证了DXR在合成生物学中的应用潜力。
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**注意**：以上文献为示例，实际研究中请通过PubMed、Web of Science或Google Scholar等平台检索真实文献(关键词：DXR, reductoisomerase, recombinant protein, metabolic engineering)。
**Background of DXR Recombinant Protein**
DXR (1-deoxy-D-xylulose 5-phosphate reductoisomerase) is a critical enzyme in the methylerythritol phosphate (MEP) pathway, a metabolic route responsible for synthesizing isoprenoid precursors in bacteria, apicomplexan parasites (e.g., *Plasmodium* spp.), and plants. Isoprenoids are essential for cellular processes such as membrane stability, hormone production, and electron transport. Unlike humans, which rely on the mevalonate pathway for isoprenoid biosynthesis, organisms dependent on the MEP pathway make DXR an attractive target for antimicrobial and antimalarial drug development.
Recombinant DXR proteins are engineered through genetic cloning and expression in heterologous systems like *E. coli* or yeast. This enables large-scale production for structural and functional studies. Researchers focus on elucidating DXR’s catalytic mechanism, substrate binding, and inhibition strategies. Fosmidomycin, a natural antibiotic, is a known DXR inhibitor and has been studied as a potential antimalarial agent, though resistance and pharmacokinetic limitations highlight the need for novel derivatives.
In structural biology, DXR’s crystal structure has been resolved, revealing a NADPH-binding domain and a catalytic site that accommodates its substrate, 1-deoxy-D-xylulose 5-phosphate (DXP). These insights guide rational drug design. Additionally, recombinant DXR is used in enzyme activity assays to screen inhibitors and optimize therapeutic candidates.
Beyond drug discovery, DXR recombinant proteins have applications in metabolic engineering. For example, enhancing isoprenoid production in microbes or plants could improve yields of bioactive compounds (e.g., artemisinin) or biofuels. However, challenges like enzyme stability and regulatory hurdles remain.
Overall, DXR recombinant protein research bridges biochemistry, medicine, and biotechnology, offering solutions to global health issues like antibiotic resistance and malaria while advancing sustainable bioproduction platforms.
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