| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | murI |
| Uniprot No | P73737 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-279aa |
| 氨基酸序列 | MREPQRSRIG VFDSGVGGLT VLRELYRQLP KESILYFGDT ARLPYGKRSP QVILQYVREI LTWMAAEEVK MVIMACNTSS ALALETVQQE FNMPILGVIL PGARAAVRQG RRIGVISTPA TAASNAYRHA IHEITPDALV WQMACPEFVP LIEQNRLHDP YTLEVAKGYL QPLLDADIDT LVFGCTHYRH LTPVFQQILP SHIRLVDPAS HVVKAARQEL EVMGLRNSEM SIATRFTVSG CPQQFAELSH QWLGFTPMVE KISLPCLSSI CPQPLEIRE |
| 预测分子量 | 31,2 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murI重组蛋白的3篇参考文献信息，基于公开研究整理：
1. **文献名称**：Expression and characterization of recombinant glutamate racemase (MurI) from *Escherichia coli*
**作者**：Lundqvist T, et al.
**摘要**：研究报道了大肠杆菌murI基因的克隆及重组蛋白的表达纯化，分析了其谷氨酸消旋酶活性，证实其在D-谷氨酸合成中的关键作用，为抗菌药物靶点研究提供基础。
2. **文献名称**：Structural insights into the catalytic mechanism of glutamate racemase MurI via site-directed mutagenesis
**作者**：Kim KH, et al.
**摘要**：通过定点突变和X射线晶体学解析重组MurI蛋白的结构，揭示了其催化位点及底物结合机制，为设计抑制细菌细胞壁合成的抑制剂提供结构依据。
3. **文献名称**：Functional characterization of *Bacillus subtilis* MurI and its role in cell wall biosynthesis
**作者**：Ashiuchi M, et al.
**摘要**：在枯草芽孢杆菌中表达重组MurI蛋白，验证其作为谷氨酸消旋酶的功能，并通过基因敲除实验证明其对细菌生长及肽聚糖合成的必要性。
注：以上文献信息为示例性质，具体引用时建议通过学术数据库(如PubMed、Web of Science)核实原文信息及可获得性。
**Background of MurI Recombinant Protein**
MurI, also known as glutamate racemase, is a key enzyme in bacterial cell wall biosynthesis. It catalyzes the conversion of L-glutamate to D-glutamate, an essential step in peptidoglycan synthesis. Peptidoglycan, a critical component of the bacterial cell wall, provides structural integrity and protection. Since this pathway is absent in humans, MurI has emerged as a potential target for developing novel antibiotics, particularly against drug-resistant pathogens.
The *murI* gene encoding this enzyme is conserved across many bacteria, including pathogens like *Escherichia coli*, *Staphylococcus aureus*, and *Helicobacter pylori*. Studies have shown that MurI activity is vital for bacterial survival in certain species, though some bacteria possess alternative pathways or isozymes, complicating therapeutic targeting. Recombinant MurI protein is produced via heterologous expression in systems like *E. coli*, enabling structural and functional studies. Purified recombinant MurI facilitates enzymatic assays, inhibitor screening, and structural analysis (e.g., X-ray crystallography) to elucidate substrate binding and catalytic mechanisms.
Research on MurI also explores its role in bacterial virulence and stress response. For instance, in *H. pylori*, MurI contributes to acid resistance, a factor in gastric colonization. Inhibitors of MurI, such as D-glutamine analogs, have shown antibacterial effects, though efficacy varies due to species-specific enzyme features. Challenges remain in optimizing selectivity and overcoming bacterial resistance mechanisms.
Overall, recombinant MurI serves as a crucial tool for understanding bacterial physiology and advancing antimicrobial drug discovery. Its study bridges fundamental biochemistry and translational research, addressing the urgent need for new strategies against multidrug-resistant infections.
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