纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RFK |
Uniprot No | Q969G6 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-155aa |
氨基酸序列 | MRHLPYFCRGQVVRGFGRGSKQLGIPTANFPEQVVDNLPADISTGIYYGWASVGSGDVHKMVVSIGWNPYYKNTKKSMETHIMHTFKEDFYGEILNVAIVGYLRPEKNFDSLESLISAIQGDIEEAKKRLELPEHLKIKEDNFFQVSKSKIMNGH |
预测分子量 | 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. |
以下是关于重组RFK(核黄素激酶)的模拟参考文献示例,供参考。请注意,这些文献为示例性质,建议通过学术数据库(如PubMed、Google Scholar)查询真实文献:
---
1. **文献名称**:*Heterologous Expression and Characterization of Recombinant Riboflavin Kinase from Escherichia coli*
**作者**:Wang, L., et al.
**摘要**:本研究报道了大肠杆菌源RFK基因的克隆、表达及纯化。重组蛋白在可溶形式下表达,经酶动力学分析显示其对核黄素的高亲和力,为后续酶学机制研究奠定基础。
2. **文献名称**:*Structural Insights into the Catalytic Mechanism of Human Riboflavin Kinase through X-ray Crystallography*
**作者**:Johnson, R., et al.
**摘要**:通过X射线晶体学解析了重组人源RFK的三维结构,揭示了其与ATP和核黄素结合的活性位点特征,并阐明了磷酸转移反应的分子机制。
3. **文献名称**:*Engineering Thermostable Riboflavin Kinase for Industrial FMN Production*
**作者**:Chen, H., et al.
**摘要**:利用定向进化技术改良重组RFK的热稳定性与催化效率,成功应用于大规模FMN生物合成,显著提高了工业生产的效率。
4. **文献名称**:*Functional Comparison of Recombinant RFK Homologs from Pathogenic Bacteria*
**作者**:Martinez, P., et al.
**摘要**:对比多种致病菌来源的重组RFK酶活性差异,发现其底物特异性与细菌代谢适应性相关,为抗菌药物靶点筛选提供依据。
---
如需具体文献,建议检索关键词如 **"recombinant riboflavin kinase expression"** 或 **"RFK structural analysis"**,并结合实际研究需求筛选。
**Background of Recombinant Riboflavin Kinase (RFK)**
Recombinant Riboflavin Kinase (RFK) is an engineered enzyme central to flavin mononucleotide (FMN) biosynthesis, catalyzing the ATP-dependent phosphorylation of riboflavin (vitamin B2) to produce FMN. FMN serves as a precursor for flavin adenine dinucleotide (FAD), both critical cofactors in redox reactions, energy metabolism, and cellular respiration. Native RFK is found across prokaryotes and eukaryotes, but recombinant versions are produced via genetic engineering to enhance yield, purity, and functionality for research and industrial applications.
The development of recombinant RFK leverages heterologous expression systems, such as *E. coli* or yeast, where the RFK gene is cloned into expression vectors and overexpressed. This approach allows scalable production, avoids contamination from native host metabolites, and enables protein modification (e.g., tagging for purification). Recombinant RFK is vital in metabolic studies, particularly in elucidating flavin-dependent pathways and addressing riboflavin metabolism disorders.
Industrially, recombinant RFK supports microbial engineering for overproducing riboflavin in biotechnology, a key additive in food and pharmaceuticals. It also aids in drug discovery, targeting pathogens reliant on flavin biosynthesis. Structural studies using recombinant RFK (e.g., X-ray crystallography) have revealed catalytic mechanisms and substrate-binding sites, guiding rational enzyme design for improved stability or activity.
Overall, recombinant RFK exemplifies the synergy between enzymology and biotechnology, offering tools to advance basic science, industrial processes, and therapeutic innovation. Its versatility continues to drive research in metabolic engineering and flavoprotein-related diseases.
×