| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pyrB |
| Uniprot No | B7MLQ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-311aa |
| 氨基酸序列 | MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSFETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFSGNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKFDGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSEYANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQALLALVLNRDLVL |
| 预测分子量 | 41.9 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pyrB重组蛋白的3篇参考文献及摘要概括：
1. **文献名称**：*Heterologous Expression and Characterization of Aspartate Transcarbamoylase (pyrB) from* Escherichia coli
**作者**：Smith J. et al.
**摘要**：研究报道了在大肠杆菌中异源表达pyrB编码的天冬氨酸氨甲酰转移酶(ATCase)，并通过亲和层析纯化获得高活性重组蛋白。酶动力学分析表明其催化效率与天然酶相似，为后续酶学机制研究提供基础。
2. **文献名称**：*Crystal Structure of Recombinant PyrB Reveals Substrate Binding Mechanism*
**作者**：Lee H. et al.
**摘要**：通过X射线晶体学解析了重组pyrB蛋白的三维结构，揭示了其底物(天冬氨酸和氨甲酰磷酸)结合位点的构象变化，阐明了催化反应中关键氨基酸残基的作用机制。
3. **文献名称**：*Optimization of pyrB Expression in* Bacillus subtilis *for Enhanced Pyrimidine Biosynthesis*
**作者**：Zhang R. et al.
**摘要**：通过启动子工程和发酵条件优化，在枯草芽孢杆菌中实现重组pyrB的高效表达，显著提升嘧啶前体合成效率，为工业微生物生产嘧啶类化合物提供策略。
4. **文献名称**：*Functional Analysis of pyrB Mutants in* Pseudomonas aeruginosa
**作者**：Martinez L. et al.
**摘要**：构建了pyrB点突变的重组蛋白，发现特定突变体导致酶活性丧失，并影响病原菌的嘧啶代谢和毒力，为抗感染药物靶点研究提供依据。
(注：以上文献信息为示例，实际引用需以具体论文为准。)
**Background of pyrB Recombinant Protein**
The *pyrB* gene encodes aspartate transcarbamoylase (ATCase), a key enzyme in the pyrimidine biosynthesis pathway. ATCase catalyzes the condensation of carbamoyl phosphate and aspartate to form N-carbamoyl aspartate, a critical step in de novo pyrimidine nucleotide production. This reaction is tightly regulated due to the essential role of pyrimidines in DNA/RNA synthesis and cellular metabolism. In bacteria, ATCase is often part of a multi-enzyme complex, while in eukaryotes, it is a distinct domain within the multifunctional CAD protein.
Recombinant pyrB proteins are produced via genetic engineering, typically by expressing the *pyrB* gene in heterologous hosts like *Escherichia coli*. This approach allows large-scale production of pure, functional ATCase for structural and biochemical studies. The enzyme’s allosteric regulation—inhibited by pyrimidine nucleotides (e.g., CTP) and activated by purine nucleotides (e.g., ATP)—has made it a model for understanding feedback inhibition and conformational changes in enzymes.
Research on recombinant pyrB proteins has provided insights into catalytic mechanisms, substrate specificity, and evolutionary conservation across species. Structural analyses (e.g., X-ray crystallography) have revealed its multi-subunit architecture and regulatory binding sites. Additionally, pyrB recombinant proteins are explored for biotechnological applications, such as enzyme engineering for industrial biocatalysis or as targets for antimicrobial drugs, since pyrimidine biosynthesis is absent in humans but vital for pathogens.
Overall, pyrB recombinant proteins serve as valuable tools for advancing both basic science and applied research in metabolism, enzymology, and drug development.
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