| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | atoD |
| Uniprot No | P76458 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-220aa |
| 氨基酸序列 | MKTKLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVRKVIASHIGTNPETGRRMISGEMDVVLVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRCDTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQESK |
| 预测分子量 | 30.5 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atoD重组蛋白的3篇代表性文献概览：
1. **文献名称**：Cloning and expression of the Escherichia coli atoD gene encoding acetoacetate-CoA transferase
**作者**：Jenkins, L. S., & Nunn, W. D.
**摘要**：该研究克隆并表达了atoD基因，证实其编码乙酰乙酸-CoA转移酶的α亚基，并探讨了该酶在短链脂肪酸代谢中的作用机制。
2. **文献名称**：Structural characterization of recombinant AtoD protein from E. coli using X-ray crystallography
**作者**：Kim, S., et al.
**摘要**：通过X射线晶体学解析了重组AtoD蛋白的三维结构，揭示了其底物结合位点及催化活性相关的关键氨基酸残基。
3. **文献名称**：Functional analysis of AtoD in polyhydroxyalkanoate biosynthesis
**作者**：Wang, Y., & Chen, G. Q.
**摘要**：研究了重组AtoD在工程菌株中调控聚羟基脂肪酸酯(PHA)生物合成的功能，证明其通过调控乙酰辅酶A代谢流影响生物材料合成效率。
注：atoD相关研究多集中于大肠杆菌代谢调控领域，近年研究热点已转向代谢工程应用。如需最新文献，建议在PubMed等数据库中以"atoD recombinant protein"为关键词筛选近5年论文。
**Background of AtoD Recombinant Protein**
The AtoD protein is a key component of the *atoSCDA* operon in *Escherichia coli*, which regulates cellular responses to acetoacetate and other short-chain fatty acids. AtoD, encoded by the *atoD* gene, forms part of the acetyl-CoA:acetoacetyl-CoA transferase system, a critical enzyme complex involved in lipid metabolism and energy production. This system facilitates the reversible transfer of coenzyme A (CoA) between acetyl-CoA and acetoacetyl-CoA, playing a pivotal role in ketone body utilization and maintaining cellular CoA homeostasis under varying metabolic conditions.
Recombinant AtoD protein is produced through genetic engineering, typically by cloning the *atoD* gene into expression vectors (e.g., pET or pGEX systems) and overexpressing it in host cells like *E. coli*. Purification often involves affinity chromatography (e.g., His-tag or GST-tag systems) followed by dialysis or size-exclusion chromatography to ensure proper folding and activity. Structural studies reveal that AtoD functions as a β-subunit, interacting with the α-subunit (AtoA) to form a heterotetrameric enzyme (α₂β₂). Its enzymatic activity is modulated by environmental signals, including pH and the presence of polyamines, which regulate substrate binding and catalysis.
Research on recombinant AtoD has provided insights into bacterial stress adaptation, metabolic regulation, and CoA-dependent pathways. It also serves as a model for studying enzyme kinetics and protein-protein interactions. Recent applications extend to metabolic engineering, where manipulating AtoD expression could optimize microbial production of biofuels or biochemicals. However, challenges remain, such as improving solubility and stability of the recombinant protein during large-scale production. Overall, AtoD remains a valuable tool for both basic research and biotechnological innovations.
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