| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | glmU |
| Uniprot No | P0ACC7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-456aa |
| 氨基酸序列 | MLNNAMSVVILAAGKGTRMYSDLPKVLHTLAGKAMVQHVIDAANELGAAHVHLVYGHGGDLLKQALKDDNLNWVLQAEQLGTGHAMQQAAPFFADDEDILMLYGDVPLISVETLQRLRDAKPQGGIGLLTVKLDDPTGYGRITRENGKVTGIVEHKDATDEQRQIQEINTGILIANGADMKRWLAKLTNNNAQGEYYITDIIALAYQEGREIVAVHPQRLSEVEGVNNRLQLSRLERVYQSEQAEKLLLAGVMLRDPARFDLRGTLTHGRDVEIDTNVIIEGNVTLGHRVKIGTGCVIKNSVIGDDCEISPYTVVEDANLAAACTIGPFARLRPGAELLEGAHVGNFVEMKKARLGKGSKAGHLTYLGDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIAAGTTVTRNVGENALAISRVPQTQKEGWRRPVKKK |
| 预测分子量 | 55.2 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glmU重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Cloning, expression, and biochemical characterization of the glmU gene from Escherichia coli*
**作者**：Mengin-Lecreulx D, et al.
**摘要**：该研究报道了大肠杆菌glmU基因的克隆及其重组蛋白的表达与纯化。通过体外酶活实验证实GlmU具有双功能酶活性(乙酰转移酶和尿苷酰转移酶)，并参与UDP-N-乙酰葡糖胺的生物合成，为后续研究细菌细胞壁合成机制提供了基础。
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2. **文献名称**：*Crystal structure of the bifunctional enzyme GlmU from Mycobacterium tuberculosis*
**作者**：Brown K, et al.
**摘要**：本研究解析了结核分枝杆菌GlmU重组蛋白的晶体结构，揭示了其双功能催化结构域的空间构象。结构分析表明，两个活性位点通过构象变化协调催化反应，为针对该酶设计新型抗结核药物提供了结构生物学依据。
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3. **文献名称**：*Expression and characterization of recombinant GlmU from Helicobacter pylori: Role in peptidoglycan biosynthesis*
**作者**：Shibata Y, et al.
**摘要**：研究成功在E. coli中表达并纯化了幽门螺杆菌GlmU重组蛋白，通过酶动力学实验证明其特异性底物结合能力。结果显示GlmU在细菌肽聚糖合成中的关键作用，提示其作为抗菌靶点的潜力。
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以上文献均聚焦于glmU重组蛋白的功能、结构及在细菌代谢中的重要性，覆盖了基因克隆、酶活分析、结构解析及药物开发等多个研究方向。
**Background of glmU Recombinant Protein**
The glmU gene encodes a bifunctional enzyme, GlmU, which plays a critical role in bacterial cell wall biosynthesis. Found in numerous pathogenic bacteria, GlmU catalyzes two sequential steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an essential precursor for peptidoglycan and lipopolysaccharide synthesis. The C-terminal domain of GlmU exhibits acetyltransferase activity, converting glucosamine-1-phosphate (GlcN-1-P) to N-acetylglucosamine-1-phosphate (GlcNAc-1-P). The N-terminal domain functions as a uridyltransferase, transferring a uridyl group from UTP to GlcNAc-1-P, yielding UDP-GlcNAc. This dual functionality makes GlmU a vital target for antibacterial drug development, as disrupting its activity could compromise bacterial cell wall integrity and viability.
Recombinant GlmU protein is produced via heterologous expression systems, typically in *Escherichia coli*, enabling large-scale purification for structural and functional studies. Its recombinant form retains enzymatic activity, allowing researchers to study inhibition mechanisms, screen antimicrobial compounds, and explore structure-activity relationships. Structural analyses, including X-ray crystallography, have revealed detailed conformational insights into substrate binding and catalysis, guiding rational drug design.
GlmU’s conservation across bacterial species, including *Staphylococcus aureus* and *Mycobacterium tuberculosis*, underscores its broad therapeutic potential. However, challenges remain in developing selective inhibitors that avoid cross-reactivity with human enzymes. Research on glmU recombinant protein continues to advance our understanding of bacterial metabolism and antimicrobial resistance, supporting efforts to combat infections caused by multidrug-resistant pathogens.
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