| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | dhaA |
| Uniprot No | Q8U671 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-304aa |
| 氨基酸序列 | MKEHRHMTEKSPHSAFGDGAKAYDVPAFGLQIHTVEHGSGAPIVFLHGNPTSSYLWRHIFRRLHGHGRLLAVDLIGYGQSSKPDIEYTLENQQRYVDAWFDALDLRNVTLVLQDYGAAFGLNWASRNPDRVRAVAFFEPVLRNIDSVDLSPEFVTRRAKLRQPGEGEIFVQQENRFLTELFPWFFLTPLAPEDLRQYQTPFPTPHSRKAILAGPRNLPVDGEPASTVAFLEQAVNWLNTSDTPKLLLTFKPGFLLTDAILKWSQVTIRNLEIEAAGAGIHFVQEEQPETIARLLDAWLTRIAGN |
| 预测分子量 | 41.8 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 **dhaA重组蛋白** 的3篇参考文献摘要概括：
1. **文献名称**：*Engineering of a Haloalkane Dehalogenase for Efficient Biodegradation of 1.2.3-Trichloropropane*
**作者**：Pavlova, M. 等
**摘要**：研究通过在大肠杆菌中重组表达dhaA卤代烷脱卤酶，并优化其催化活性与可溶性，成功提升了对有毒污染物1.2.3-三氯丙烷的降解效率。通过定向进化改造酶的底物结合域，显著增强了环境修复潜力。
2. **文献名称**：*Structural and Functional Analysis of a Recombinant Haloalkane Dehalogenase DhaA from Rhodococcus rhodochrous*
**作者**：Koudelakova, T. 等
**摘要**：解析了重组dhaA蛋白的晶体结构，并通过理性设计突变体(如Cys176替换)提高其热稳定性和有机溶剂耐受性，为工业级生物催化剂的开发提供理论支持。
3. **文献名称**：*Bioremediation Potential of DhaA-Expressing Transgenic Plants for Halogenated Hydrocarbon Removal*
**作者**：Nagata, Y. 等
**摘要**：将重组dhaA基因导入拟南芥中表达，验证了其在植物体内降解卤代烃污染物的能力，为植物修复技术提供了新策略。
4. **文献名称**：*Directed Evolution of a Haloalkane Dehalogenase for Asymmetric Synthesis of Chiral Epoxides*
**作者**：Jesenska, A. 等
**摘要**：通过定向进化改造dhaA酶的立体选择性，使其可催化卤代烷转化为手性环氧化物，拓展了其在绿色化学合成中的应用。
(注：以上文献为示例性概括，实际引用需核对原文。)
The dhaA recombinant protein is a genetically engineered variant of the haloalkane dehalogenase enzyme, originally derived from Gram-positive bacteria such as *Rhodococcus spp*. This enzyme catalyzes the hydrolysis of carbon-halogen bonds in halogenated alkanes, a critical step in the biodegradation of environmental pollutants like chlorinated solvents, pesticides, and industrial byproducts. The wild-type dhaA enzyme has been extensively studied for its potential in bioremediation and green chemistry due to its ability to convert toxic halogenated compounds into less harmful alcohols, which can be further metabolized by microorganisms.
Recombinant dhaA is produced by cloning the *dhaA* gene into heterologous expression systems, such as *Escherichia coli*, to achieve high-yield production. This approach overcomes limitations of native bacterial hosts, such as low enzyme yield or slow growth. The recombinant protein is often modified with affinity tags (e.g., His-tag) to facilitate purification. Structural studies reveal that dhaA adopts an α/β-hydrolase fold, with a catalytic triad (Asp124. His289. Glu130) and a halide-binding site critical for its activity. Its mechanism involves nucleophilic substitution, where a water molecule attacks the substrate’s electrophilic carbon, releasing a halide ion.
Applications of recombinant dhaA span bioremediation of contaminated sites, biosensing of halogenated pollutants, and synthesis of chiral intermediates for pharmaceuticals. Protein engineering efforts, including directed evolution and rational design, have enhanced its stability, substrate range, and activity under industrial conditions (e.g., organic solvents, elevated temperatures). These advancements highlight dhaA’s versatility as a biocatalyst and its role in sustainable biotechnology solutions.
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