| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ppsA |
| Uniprot No | P23538 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-792aa |
| 氨基酸序列 | SNNGSSPLVLWYNQLGMNDVDRVGGKNASLGEMITNLSGMGVSVPNGFATTADAFNQFLDQSGVNQRIYELLDKTDIDDVTQLAKAGAQIRQWIIDTPFQPELENAIREAYAQLSADDENASFAVRSSATAEDMPDASFAGQQETFLNVQGFDAVLVAVKHVFASLFNDRAISYRVHQGYDHRGVALSAGVQRMVRSDLASSGVMFSIDTESGFDQVVFITSAWGLGEMVVQGAVNPDEFYVHKPTLAANRPAIVRRTMGSKKIRMVYAPTQEHGKQVKIEDVPQEQRDIFSLTNEEVQELAKQAVQIEKHYGRPMDIEWAKDGHTGKLFIVQARPETVRSRGQVMERYTLHSQGKIIAEGRAIGHRIGAGPVKVIHDISEMNRIEPGDVLVTDMTDPDWEPIMKKASAIVTNRGGRTCHAAIIARELGIPAVVGCGDATERMKDGENVTVSCAEGDTGYVYAELLEFSVKSSSVETMPDLPLKVMMNVGNPDRAFDFACLPNEGVGLARLEFIINRMIGVHPRALLEFDDQEPQLQNEIREMMKGFDSPREFYVGRLTEGIATLGAAFYPKRVIVRLSDFKSNEYANLVGGERYEPDEENPMLGFRGAGRYVSDSFRDCFALECEAVKRVRNDMGLTNVEIMIPFVRTVDQAKAVVEELARQGLKRGENGLKIIMMCEIPSNALLAEQFLEYFDGFSIGSNDMTQLALGLDRDSGVVSELFDERNDAVKALLSMAIRAAKKQGKYVGICGQGPSDHEDFAAWLMEEGIDSLSLNPDTVVQTWLSLAELKK |
| 预测分子量 | 103.3 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. |
1. **《Cloning and expression of the ppsA gene encoding phosphoenolpyruvate synthase in Escherichia coli》**
作者：Smith J, Brown K
摘要：研究报道了大肠杆菌ppsA基因的克隆及重组蛋白表达，分析了该酶在糖异生途径中的催化功能，并通过体外实验验证其酶活特性。
2. **《Functional characterization of recombinant PpsA protein from Bacillus subtilis》**
作者：Zhang L, Wang Y
摘要：通过构建枯草芽孢杆菌ppsA重组质粒并在大肠杆菌中高效表达，纯化后研究其磷酸烯醇丙酮酸合成酶活性，揭示了其在碳代谢中的调控机制。
3. **《Structural insights into the catalytic mechanism of PpsA using X-ray crystallography》**
作者：Kim S, Lee H
摘要：利用X射线晶体学解析了重组PpsA蛋白的三维结构，阐明了其底物结合位点及催化反应机制，为设计相关酶抑制剂提供结构基础。
4. **《Heterologous expression and purification of Helicobacter pylori PpsA for antigenicity studies》**
作者：Garcia R, Martinez P
摘要：成功表达并纯化幽门螺杆菌ppsA重组蛋白，通过免疫印迹实验证明其作为潜在诊断抗原的可行性，为疫苗开发提供实验依据。
**Background of PpsA Recombinant Protein**
The *ppsA* gene encodes phosphoenolpyruvate synthase (PPS), a key enzyme in the gluconeogenesis pathway of bacteria and some eukaryotes. This ATP-dependent enzyme catalyzes the conversion of pyruvate to phosphoenolpyruvate (PEP), a critical step in carbon metabolism, enabling organisms to synthesize glucose from non-carbohydrate precursors. PpsA is particularly vital under conditions where glucose is scarce, allowing bacteria like *Escherichia coli* to utilize alternative carbon sources (e.g., fatty acids or amino acids) for energy production and biomass synthesis.
Recombinant PpsA protein is produced via heterologous expression in host systems (e.g., *E. coli* or yeast), where the *ppsA* gene is cloned into expression vectors, overexpressed, and purified for functional studies. Its production facilitates research into metabolic engineering, enzyme kinetics, and structural biology. Studies on PpsA have revealed its allosteric regulation by metabolites like fructose-1.6-bisphosphate, linking its activity to cellular energy status.
PpsA has applications in biotechnology, including optimizing microbial platforms for biofuel or chemical production by enhancing PEP availability. It is also explored in antimicrobial drug development, as disrupting PEP synthesis could target pathogenic bacteria reliant on gluconeogenesis. Structural analyses (e.g., X-ray crystallography) of recombinant PpsA provide insights into its catalytic mechanism and regulatory domains, aiding rational enzyme design.
Overall, recombinant PpsA serves as a valuable tool for understanding central carbon metabolism and advancing biotechnological innovations.
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