| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ldcA |
| Uniprot No | P76008 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-304aa |
| 氨基酸序列 | MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM |
| 预测分子量 | 37.6 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 **ldcA重组蛋白** 的示例参考文献(内容为模拟示例，建议通过学术数据库验证原文)：
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1. **文献名称**: "Cloning and characterization of the ldcA gene encoding lysine decarboxylase in Escherichia coli"
**作者**: Lee JH, et al.
**摘要**: 本研究克隆并表达了来自大肠杆菌的ldcA基因，验证其编码的赖氨酸脱羧酶活性。实验表明，重组LdcA蛋白在低pH条件下显著增强细菌的酸耐受性，并催化赖氨酸生成尸胺(cadaverine)。
2. **文献名称**: "Heterologous expression and biotechnological application of ldcA in synthetic biology"
**作者**: Shi H, et al.
**摘要**: 通过在大肠杆菌中重组表达ldcA基因，优化了赖氨酸脱羧酶的产量和活性。该研究展示了重组LdcA在体外合成尸胺的潜力，为生物基聚酰胺材料生产提供了新策略。
3. **文献名称**: "Structural insights into the catalytic mechanism of recombinant LdcA from Salmonella typhimurium"
**作者**: Zhang Y, et al.
**摘要**: 解析了重组沙门氏菌LdcA蛋白的晶体结构，揭示了其依赖磷酸吡哆醛(PLP)的催化机制，并通过定点突变验证了关键氨基酸残基在底物结合中的作用。
4. **文献名称**: "Metabolic engineering of E. coli using ldcA for enhanced acid resistance and industrial fermentation"
**作者**: Wang L, et al.
**摘要**: 通过过表达重组ldcA基因改造大肠杆菌代谢通路，显著提高了菌株在工业发酵中的酸耐受性和产物(如丁酸)的合成效率。
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建议通过 **PubMed/Google Scholar** 搜索关键词 `ldcA recombinant protein` 或 `lysine decarboxylase expression` 获取真实文献。
The ldcA gene encodes lysine decarboxylase, a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes the decarboxylation of L-lysine to produce cadaverine and carbon dioxide. This enzyme plays a critical role in bacterial acid resistance and metabolic adaptation, particularly in enteric pathogens like Escherichia coli and Salmonella enterica. Under acidic conditions, ldcA is upregulated as part of the acid response system, neutralizing intracellular pH by consuming protons during the decarboxylation reaction. The resulting cadaverine, a polyamine, also contributes to membrane stability and stress tolerance.
Recombinant ldcA protein is engineered through heterologous expression systems (e.g., E. coli or yeast) for biochemical and structural studies. Its hexameric quaternary structure and pH-dependent activity have been characterized to understand substrate specificity and catalytic mechanisms. Researchers focus on ldcA due to its dual relevance in bacterial pathogenesis and industrial applications. In pathogenic bacteria, ldcA-mediated acid resistance enhances survival in host gastrointestinal tracts, making it a potential antimicrobial target. Industrially, the enzyme attracts interest for bio-based production of cadaverine, a precursor for bio-polyamides and green plastics.
Studies on recombinant ldcA also explore its biotechnological optimization, including thermostability engineering and pH robustness, to improve efficiency in synthetic biology workflows. Additionally, structural insights from recombinant protein crystallography aid in designing inhibitors to disrupt bacterial acid tolerance. The enzyme’s ability to function under mild conditions aligns with sustainable chemistry goals, positioning ldcA as a versatile tool in both medical research and industrial biocatalysis. Ongoing research aims to balance its catalytic efficiency with stability for scalable applications.
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