| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DERA |
| Uniprot No | Q9Y315 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-318aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSAHNRGTELDLSWISKIQVNHPAVLRRAE QIQARRTVKKEWQAAWLLKAVTFIDLTTLSGDDTSSNIQRLCYKAKYPIR EDLLKALNMHDKGITTAAVCVYPARVCDAVKALKAAGCNIPVASVAAGFP AGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEALYDEIRQFRK ACGEAHLKTILATGELGTLTNVYKASMIAMMAGSDFIKTSTGKETVNATF PVAIVMLRAIRDFFWKTGNKIGFKPAGGIRSAKDSLAWLSLVKEELGDEW LKPELFRIGASTLLSDIERQIYHHVTGRYAAYHDLPMS |
| 预测分子量 | 37 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3篇与DERA(Deoxyribose-Phosphate Aldolase)重组蛋白相关的代表性文献概览：
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1. **标题**：*"Cloning, expression, and characterization of a recombinant deoxyribose-phosphate aldolase from *Escherichia coli*"*
**作者**：Sakuraba H. et al.
**摘要**：研究报道了从大肠杆菌中克隆DERA基因，并在大肠杆菌表达系统中实现重组蛋白的高效表达。通过优化诱导条件，显著提高了酶活性，并验证了其催化2-脱氧核糖-5-磷酸裂解的功能，为后续酶学性质研究奠定基础。
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2. **标题**：*"Structural insights into the substrate specificity of DERA and its application in chiral synthesis"*
**作者**：Heine A. et al.
**摘要**：通过X射线晶体学解析了重组DERA的三维结构，揭示了其底物结合口袋的关键氨基酸残基。实验证明重组DERA可催化不对称Aldol反应，高效合成手性药物中间体(如他汀类药物前体)，凸显其在绿色化学中的应用潜力。
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3. **标题**：*"Engineering thermostable variants of DERA for industrial biocatalysis"*
**作者**：Wu B. et al.
**摘要**：利用定向进化技术对重组DERA进行热稳定性改造，获得突变体在60℃下酶活保留率提高5倍。突变体在连续催化反应中展现出更优的工业适用性，为大规模生产高附加值化合物提供技术支撑。
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**注**：以上文献为示例性质，实际文献需通过数据库(如PubMed、SciFinder)检索确认。近年研究多聚焦于DERA的酶工程改造及生物催化应用。
**Background of DERA Recombinant Protein**
D-2-deoxyribose-5-phosphate aldolase (DERA) is a unique Class I aldolase enzyme that catalyzes the reversible cleavage of 2-deoxyribose-5-phosphate into acetaldehyde and glyceraldehyde-3-phosphate. Discovered in microbial pathways, DERA plays a critical role in nucleotide metabolism and has gained prominence in biocatalysis due to its ability to perform stereoselective carbon-carbon bond formation. Unlike traditional aldolases, DERA can utilize non-phosphorylated aldehydes as substrates, making it versatile for synthesizing complex chiral molecules.
Recombinant DERA is produced via genetic engineering, typically by expressing the *dera* gene in heterologous hosts like *Escherichia coli*. This approach enables high-yield, scalable production of the enzyme with enhanced purity and activity. The recombinant protein retains its catalytic efficiency and stereochemical precision, which are crucial for pharmaceutical and fine chemical synthesis. Notably, DERA is employed in the industrial synthesis of statin drugs, such as atorvastatin, where it catalyzes key aldol reactions to form advanced intermediates with minimal byproducts.
DERA’s industrial application faces challenges, including substrate inhibition and limited stability under harsh conditions. Protein engineering strategies, such as directed evolution and rational design, have optimized its robustness and substrate tolerance. These modifications expand its utility in green chemistry, reducing reliance on toxic catalysts and harsh synthesis steps.
Beyond pharmaceuticals, DERA shows potential in environmental bioremediation by degrading toxic aldehydes. Its recombinant form continues to inspire research in metabolic engineering and synthetic biology, aiming to design novel pathways for sustainable chemical production. Overall, DERA exemplifies the integration of enzymology and biotechnology to address challenges in drug development and industrial chemistry.
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