| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DHPS |
| Uniprot No | P49366 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-369aa |
| 氨基酸序列 | MEGSLEREAP AGALAAVLKH SSTLPPESTQ VRGYDFNRGV NYRALLEAFG TTGFQATNFG RAVQQVNAMI EKKLEPLSQD EDQHADLTQS RRPLTSCTIF LGYTSNLISS GIRETIRYLV QHNMVDVLVT TAGGVEEDLI KCLAPTYLGE FSLRGKELRE NGINRIGNLL VPNENYCKFE DWLMPILDQM VMEQNTEGVK WTPSKMIARL GKEINNPESV YYWAQKNHIP VFSPALTDGS LGDMIFFHSY KNPGLVLDIV EDLRLINTQA IFAKCTGMII LGGGVVKHHI ANANLMRNGA DYAVYINTAQ EFDGSDSGAR PDEAVSWGKI RVDAQPVKVY ADASLVFPLL VAETFAQKMD AFMHEKNED |
| 预测分子量 | 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DHPS重组蛋白的3篇参考文献示例(内容为虚构，仅供参考)：
1. **文献名称**：重组肺炎链球菌DHPS的表达、纯化及酶活性分析
**作者**：Smith J et al.
**摘要**：本研究成功在大肠杆菌中表达了重组肺炎链球菌DHPS蛋白，通过亲和层析纯化获得高纯度蛋白。酶动力学实验表明，该重组蛋白具有催化二氢蝶酸与对氨基苯甲酸结合的活性，为后续药物筛选提供了基础。
2. **文献名称**：卡氏肺孢子菌DHPS的晶体结构解析与磺胺类药物抗性机制
**作者**：Li X et al.
**摘要**：通过X射线晶体学解析了卡氏肺孢子菌DHPS重组蛋白的三维结构，发现其活性位点突变(如Pro55Ser)会导致磺胺类药物结合能力下降，揭示了临床耐药性的分子机制。
3. **文献名称**：基于重组DHPS的高通量抑制剂筛选平台的建立
**作者**：Wang Y et al.
**摘要**：利用昆虫细胞表达系统制备了高活性重组DHPS蛋白，并开发了一种基于荧光检测的酶活抑制筛选方法。该平台成功筛选出两种新型小分子抑制剂，为抗生素研发提供了新方向。
**Background of Dihydrodipicolinate Synthase (DHDPS/DHPS) Recombinant Protein**
Dihydrodipicolinate synthase (DHDPS or DHPS) is a key enzyme in the lysine biosynthesis pathway, primarily found in bacteria, plants, and some fungi. It catalyzes the first committed step of lysine production by condensing L-aspartate-β-semialdehyde (ASA) and pyruvate to form dihydrodipicolinate (DHDP). This reaction is critical for synthesizing meso-diaminopimelate (mDAP) and lysine, essential components for bacterial cell wall peptidoglycans and overall protein biosynthesis. Due to its absence in humans, DHPS has emerged as a promising target for antibiotic development, particularly against pathogenic bacteria like *Staphylococcus aureus* and *Mycobacterium tuberculosis*.
Recombinant DHPS proteins are engineered using genetic cloning techniques, where the *dapA* gene (encoding DHPS) is inserted into expression vectors (e.g., *E. coli* or yeast systems) for large-scale production. Purification methods, such as affinity chromatography, ensure high protein purity for structural and functional studies. Recombinant DHPS enables detailed investigations into enzyme kinetics, substrate specificity, and inhibitor interactions, which are crucial for rational drug design.
Studies on DHPS structure (via X-ray crystallography or cryo-EM) have revealed its homotetrameric architecture and active-site residues, providing insights into catalytic mechanisms. Additionally, recombinant variants help explore mutations linked to antibiotic resistance, such as those reducing sulfonamide drug binding in resistant bacterial strains. Beyond antimicrobial research, plant DHPS is studied to enhance crop lysine content, addressing nutritional deficiencies in staple foods.
Overall, recombinant DHPS proteins serve as vital tools for advancing antimicrobial therapies, understanding metabolic pathways, and improving agricultural biotechnology.
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