| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | purD |
| Uniprot No | Q8X612 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-429aa |
| 氨基酸序列 | MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTLQNVAIGVTDIPALLDFAQNEKVDLTIVGPEAPLVKGVVDTFRAAGMKIFGPTAGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMASEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLDEKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVEDGKVFHAGTKLADDEQVVTSGGRVLCVTALGHTVAEAQKRAYALMTDIHWDDCFCRKDIGWRAIEREQN |
| 预测分子量 | 62.0 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purD重组蛋白的3篇代表性文献的示例(内容基于典型研究方向概括，非真实文献)：
1. **文献名称**：*Cloning and Expression of the purD Gene in Escherichia coli for ATP-Dependent Phosphoribosylamine Synthesis*
**作者**：Johnson, R. et al.
**摘要**：该研究成功克隆了purD基因并在大肠杆菌中高效表达重组蛋白，验证了其催化甘氨酰胺核苷酸(GAR)转化为甲酰甘氨酰胺核苷酸(FGAR)的ATP依赖性活性，为嘌呤代谢研究提供工具。
2. **文献名称**：*Crystallographic Analysis of purD Recombinant Protein Reveals Substrate Binding Mechanism*
**作者**：Smith, L. & Phillips, G.
**摘要**：通过X射线晶体学解析了purD重组蛋白的三维结构，揭示了其与底物GAR及ATP的结合位点，阐明了催化过程中构象变化的分子机制。
3. **文献名称**：*Optimization of purD Recombinant Protein Purification Using Affinity Chromatography*
**作者**：Chen, Y. et al.
**摘要**：开发了一种基于组氨酸标签的亲和层析方法，显著提高了purD重组蛋白的纯化效率和稳定性，并验证了纯化后蛋白的酶活性和动力学参数。
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注：以上为模拟示例，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词“purD recombinant protein”获取。如需真实文献，可提供具体研究年份或领域进一步筛选。
The purD gene encodes phosphoribosylamine-glycine ligase (PurD), a key enzyme in the de novo purine biosynthesis pathway. This ATP-dependent enzyme catalyzes the second step of the pathway, converting 5-phosphoribosylamine (PRA) and glycine into glycinamide ribonucleotide (GAR), a critical precursor for inosine monophosphate (IMP) synthesis. As purine nucleotides are essential for DNA/RNA synthesis and cellular energy metabolism, PurD is evolutionarily conserved across bacteria, archaea, and eukaryotes, making it a potential therapeutic target for antimicrobial or anticancer strategies.
Recombinant PurD protein is typically produced through heterologous expression in bacterial systems like Escherichia coli. This approach enables large-scale purification and structural-functional studies that are challenging with native proteins. The recombinant protein retains enzymatic activity, allowing researchers to investigate its catalytic mechanism, ATP-binding domains, and substrate specificity. Structural analyses (e.g., X-ray crystallography) have revealed conserved motifs involved in ATP hydrolysis and PRA binding, providing insights into inhibitor design.
In antimicrobial research, bacterial PurD has gained attention due to its divergence from human enzymes in certain pathogenic species. Targeting this enzyme could lead to species-specific antibiotics with reduced off-target effects. Additionally, recombinant PurD serves as a tool for high-throughput screening of small-molecule inhibitors and for studying mutations associated with antibiotic resistance. Beyond therapeutic applications, it aids in understanding fundamental biochemical processes, including allosteric regulation and enzyme kinetics in nucleotide metabolism. Recent studies also explore its role in microbial pathogenesis and metabolic adaptation under purine-limited conditions.
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