| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | bioH |
| Uniprot No | P13001 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-256aa |
| 氨基酸序列 | MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPAEFCHLLVALKQRV |
| 预测分子量 | 35.9 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3篇关于bioH重组蛋白的参考文献及其摘要概述：
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1. **文献名称**: *"Functional Characterization of the BioH Enzyme in the Biotin Biosynthesis Pathway of Escherichia coli"*
**作者**: Lin, Y., & Cronan, J. E.
**摘要**: 本研究解析了大肠杆菌bioH基因编码的羧酸酯酶在生物素合成中的功能，通过重组表达和纯化bioH蛋白，证实其参与去除生物素前体中的甲基基团，并验证了其底物特异性。
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2. **文献名称**: *"Crystal Structure and Substrate Specificity of BioH from the Biotin Biosynthetic Pathway"*
**作者**: Tran, N., et al.
**摘要**: 通过X射线晶体学解析了重组bioH蛋白的三维结构，结合酶活实验揭示了其催化机制中关键氨基酸残基的作用，为设计基于bioH的酶工程改造提供结构基础。
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3. **文献名称**: *"Heterologous Expression and Optimization of BioH for Biotechnological Applications"*
**作者**: Zhang, R., et al.
**摘要**: 报道了在毕赤酵母系统中高效表达重组bioH蛋白的优化策略，证明其在大规模生产中可用于合成生物素类似物，拓展了其在工业酶催化中的应用潜力。
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**说明**：以上文献为虚拟示例，实际引用需检索PubMed或Web of Science等数据库获取真实文献(可尝试关键词 "bioH recombinant protein expression")。
**Background of BioH Recombinant Protein**
BioH is a key enzyme involved in bacterial biotin biosynthesis, primarily characterized in *Escherichia coli*. It functions as a carboxylesterase within the bio operon, catalyzing the hydrolysis of methyl esters in the late stages of biotin (vitamin B7) production. Biotin is an essential cofactor for central metabolic processes, including fatty acid synthesis and gluconeogenesis. While many organisms acquire biotin through diet or symbiosis, bacteria like *E. coli* synthesize it de novo, making the bio pathway a potential target for antimicrobial strategies.
The *bioH* gene encodes a 28 kDa protein that exhibits α/β-hydrolase fold architecture, typical of esterase enzymes. Its catalytic triad (Ser-His-Asp) enables substrate recognition and hydrolysis. BioH specifically processes pimeloyl-ACP methyl ester, generating pimelic acid, a precursor for the biotin side chain. Disruption of *bioH* impairs biotin synthesis, leading to auxotrophy in bacteria unless supplemented with biotin or intermediates.
Recombinant BioH protein is produced via heterologous expression in systems like *E. coli* or yeast, enabling high-yield purification for structural and functional studies. Its recombinant form retains enzymatic activity, making it valuable for biochemical assays, inhibitor screening, and metabolic engineering. Structural analyses (e.g., X-ray crystallography) have clarified substrate-binding mechanisms and guided protein engineering efforts.
Beyond its metabolic role, BioH has biotechnological applications. It serves as a model for studying esterase evolution and substrate specificity. Additionally, engineered BioH variants are explored for industrial processes, such as ester hydrolysis in biocatalysis. In synthetic biology, the bio operon, including *bioH*, is leveraged to design biotin-responsive genetic circuits for controlled gene expression.
Overall, BioH exemplifies how understanding bacterial metabolism can inform both antimicrobial development and biocatalytic tool design, bridging fundamental microbiology and applied biotechnology.
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