| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tdcD |
| Uniprot No | P59244 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-402aa |
| 氨基酸序列 | MNEFPVVLVINCGSSSIKFSVLNASDCEVLMSGIADGINSENAFLSVNGGEPAPLAHHSYEGALKAIAFELEKRNLNDNVALIGHRIAHGGSIFTESAIITDEVIDNIRRVSPLAPLHNYANLSGIESAQQLFPGVTQVAVFDTSFHQTMAPEAYLYGLPWKYYEELGVRRYGFHGTSHRYVSQRAHSLLNLAEDDSGLVVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMSWVASQTNQSLGDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERAQLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSSLIRRLVMEHLAVLGVEIDTEMNNRSNSFGERIVSSENARVICAVIPTNEEKMIALDAIHLGKVNAPAEFA |
| 预测分子量 | 50.4 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. |
以下是关于 TdcD 重组蛋白的模拟参考文献(基于公开研究背景整理，非真实文献)：
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1. **标题**: *Cloning and Characterization of Recombinant TdcD from Escherichia coli: A Threonine Deaminase with Pyruvate Decarboxylase Activity*
**作者**: Smith J, et al.
**摘要**: 本研究报道了通过大肠杆菌系统重组表达 TdcD 蛋白，验证其作为苏氨酸脱氨酶的催化功能，并发现其具有丙酮酸脱羧酶活性。通过酶动力学分析揭示了其在厌氧条件下参与氨基酸代谢的分子机制。
2. **标题**: *Structural Insights into TdcD Recombinant Protein: Implications for Substrate Specificity*
**作者**: Lee H, et al.
**摘要**: 通过X射线晶体学解析了重组 TdcD 蛋白的三维结构，揭示了其底物结合口袋的关键残基，并利用定点突变实验验证了其对苏氨酸和丙酮酸的双重底物特异性，为工程化改造提供了依据。
3. **标题**: *Optimization of Recombinant TdcD Expression in E. coli for Industrial Biocatalysis*
**作者**: Zhang Y, et al.
**摘要**: 系统优化了 TdcD 重组蛋白在大肠杆菌中的表达条件(如诱导温度、IPTG 浓度)，将酶活提高3倍，并评估了其在生物合成 α-酮丁酸中的工业化应用潜力。
4. **标题**: *Functional Interaction between TdcD and TdcE in Bacterial Amino Acid Catabolism*
**作者**: Müller R, et al.
**摘要**: 通过体外重组蛋白共表达实验，证明了 TdcD 与 TdcE 在细菌降解苏氨酸通路中的协同作用，并利用敲除菌株验证了其对细胞厌氧生长的必要性。
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注：以上文献为示例性内容，实际研究中建议通过 PubMed 或 Web of Science 以 "TdcD recombinant protein" 或 "TdcD threonine deaminase" 为关键词检索真实文献。
The tdcD recombinant protein is a key component in the threonine degradation pathway of certain bacteria, particularly in *Escherichia coli*. This protein is encoded by the *tdcD* gene, part of the *tdc operon* (threonine decarboxylase operon), which is involved in the anaerobic catabolism of L-threonine into propionate and glycine. The TdcD enzyme functions as a threonine dehydratase, catalyzing the deamination of threonine to α-ketobutyrate, a critical step in this energy-generating pathway. Unlike the aerobic threonine degradation enzyme IlvA, TdcD is specifically induced under anaerobic conditions and acidic environments, reflecting its role in bacterial survival during oxygen-limited stress, such as in the gut or during biofilm formation.
Recombinant TdcD protein is typically produced via heterologous expression in *E. coli* systems, enabling purification for biochemical and structural studies. Research on TdcD has revealed its allosteric regulation by AMP and pyruvate, which modulate its activity to align with cellular energy demands. Its unique regulatory mechanisms and substrate specificity make it a subject of interest in microbial metabolism, antibiotic development, and synthetic biology applications. Additionally, TdcD’s role in producing toxic metabolic byproducts (e.g., propionate) has implications for understanding bacterial pathogenesis and interspecies competition in microbiomes. Studies leveraging recombinant TdcD contribute to elucidating anaerobic metabolic adaptations and engineering microbial pathways for bioproduction.
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