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Recombinant E.coli PPDK protein

  • 中文名: 丙酮酸(PPDK)重组蛋白
  • 别    名: PPDK;Pyruvate, phosphate dikinase 1, chloroplastic
货号: PA2000-2629
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产品详情

纯度>90%SDS-PAGE.
种属Entamoeba
靶点PPDK
Uniprot No P37213
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-342aa
氨基酸序列MQRVYAFEDGDGTNKKLLGGKGAGLCTMTKIGLPVPQGFVITTEMCKQFIANGNKMPEGLMEEVKKEYQLVEKKSGKVFGGEENPLLVSVRSGAAMSMPGMMDTILNLGLNDKTVVALAKLTNNERFAYDSYRRFVSLFGKIALNACDEVYDKTLENKKVEKGVKLDTELDANDMKELAQVFIKKTEEFTKQPFPVDPYAQLEFAICAVFRSWMGKRAVDYRREFKITPEQADGTAVSVVSMVYGNMGNDSATGVCFTRDPGTGENMFFGEYLKNAQGEDVVAGIRTPQIISKMAEDRDLPGCYEQLLDIRKKLEGYFHEVQDFEFTIERKKLYMLQTRNGK
预测分子量 54.4 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.

参考文献

以下是3-4条关于PPDK(丙酮酸磷酸双激酶)重组蛋白的虚构参考文献示例(实际文献请通过学术数据库检索):

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1. **文献名称**: *Heterologous Expression and Characterization of Recombinant Pyruvate Phosphate Dikinase from Maize*

**作者**: Smith J, et al.

**摘要**: 研究通过大肠杆菌系统异源表达玉米PPDK重组蛋白,优化纯化条件并分析其酶活性和热稳定性,证实重组蛋白在体外可逆催化丙酮酸与磷酸烯醇式丙酮酸转化。

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2. **文献名称**: *Crystal Structure Analysis of Recombinant PPDK from Thermotoga maritima*

**作者**: Lee H, et al.

**摘要**: 解析了来自极端嗜热菌Thermotoga maritima的重组PPDK晶体结构,揭示了其活性位点关键残基及磷酸化调控机制,为酶工程改造提供结构基础。

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3. **文献名称**: *Functional Expression of PPDK in Saccharomyces cerevisiae for Metabolic Engineering*

**作者**: Chen L, et al.

**摘要**: 在酿酒酵母中表达重组PPDK,成功构建C4代谢通路模块,提升乙酰辅酶A合成效率,为合成生物学中碳代谢途径优化提供新策略。

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4. **文献名称**: *Comparative Study of Recombinant PPDK Production in Different Host Systems*

**作者**: Gupta R, et al.

**摘要**: 比较大肠杆菌、毕赤酵母和昆虫细胞系统表达PPDK的效率,发现毕赤酵母系统产率最高且酶活性稳定,适用于工业化规模制备。

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**备注**:以上文献为示例,实际研究需通过PubMed、Web of Science或Google Scholar等平台检索关键词(如“PPDK recombinant protein expression”“Pyruvate phosphate dikinase heterologous”)。

背景信息

**Background of PPDK Recombinant Protein**

Pyruvate, phosphate dikinase (PPDK) is a pivotal enzyme in plant metabolism, primarily associated with the C4 and crassulacean acid metabolism (CAM) photosynthetic pathways. It catalyzes the reversible conversion of pyruvate, ATP, and inorganic phosphate (Pi) to phosphoenolpyruvate (PEP), AMP, and pyrophosphate (PPi), a reaction critical for regenerating PEP—the primary CO2 acceptor in C4 plants. This enzyme enables C4 plants to achieve high photosynthetic efficiency under hot, arid conditions by concentrating CO2 around RuBisCO, minimizing photorespiration.

Native PPDK is a large, multi-domain protein (~95 kDa) regulated by post-translational modifications, such as reversible phosphorylation, which modulates its activity in response to light-dark cycles. However, extracting and purifying PPDK directly from plant tissues is challenging due to low abundance and complex purification requirements.

Recombinant PPDK technology addresses these limitations by expressing the enzyme in heterologous systems like *E. coli* or yeast. The PPDK gene is cloned into expression vectors, enabling scalable production with high purity and consistency. Engineered variants can also be developed to enhance stability, activity, or compatibility with industrial processes.

Recombinant PPDK has broad applications. In biotechnology, it supports efforts to engineer C4 traits into C3 crops (e.g., rice) to improve yield and stress resilience. It is also used in synthetic biology for producing PEP-dependent biochemical pathways and in industrial biocatalysis for sustainable chemical synthesis. Additionally, recombinant PPDK serves as a model for studying enzyme kinetics, allosteric regulation, and evolutionary adaptations in photosynthetic organisms.

Overall, recombinant PPDK bridges fundamental research and applied biotechnology, offering tools to advance agriculture, bioenergy, and enzymatic engineering.

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