| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | BBE1 |
| Uniprot No | P30986 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-538aa |
| 氨基酸序列 | GNDLLSCLTFNGVRNHTVFSADSDSDFNRFLHLSIQNPLFQNSLISKPSAIILPGSKEELSNTIRCIRKGSWTIRLRSGGHSYEGLSYTSDTPFILIDLMNLNRVSIDLESETAWVESGSTLGELYYAITESSSKLGFTAGWCPTVGTGGHISGGGFGMMSRKYGLAADNVVDAILIDANGAILDRQAMGEDVFWAIRGGGGGVWGAIYAWKIKLLPVPEKVTVFRVTKNVAIDEATSLLHKWQFVAEELEEDFTLSVLGGADEKQVWLTMLGFHFGLKTVAKSTFDLLFPELGLVEEDYLEMSWGESFAYLAGLETVSQLNNRFLKFDERAFKTKVDLTKEPLPSKAFYGLLERLSKEPNGFIALNGFGGQMSKISSDFTPFPHRSGTRLMVEYIVAWNQSEQKKKTEFLDWLEKVYEFMKPFVSKNPRLGYVNHIDLDLGGIDWGNKTVVNNAIEISRSWGESYFLSNYERLIRAKTLIDPNNVFNHPQSIPPMANFDYLEKTLGSDGGEVVI |
| 预测分子量 | 59.4 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BBE1重组蛋白的参考文献示例(注：以下文献为虚构，供参考格式，建议通过学术数据库检索真实文献)：
1. **文献名称**: "Cloning and heterologous expression of berberine bridge enzyme (BBE1) from *Papaver somniferum*"
**作者**: Frick, S., Kutchan, T.M.
**摘要**: 报道了从罂粟中克隆BBE1基因，并在大肠杆菌中成功表达重组蛋白，证实其催化(S)-reticuline转化为(S)-scoulerine的能力，为体外生物碱合成研究提供工具。
2. **文献名称**: "Functional characterization of recombinant BBE1 in benzylisoquinoline alkaloid biosynthesis"
**作者**: Dittrich, H., et al.
**摘要**: 通过重组BBE1蛋白的酶动力学分析，揭示其在苄基异喹啉生物碱途径中的底物特异性及pH/温度依赖性，为代谢工程优化提供依据。
3. **文献名称**: "Crystal structure of BBE1 from *Eschscholzia californica*: insights into flavin-dependent oxidase mechanism"
**作者**: Gesell, A., et al.
**摘要**: 首次解析了加州罂粟来源的BBE1重组蛋白晶体结构，阐明其依赖FAD的氧化机制及底物结合位点特征，助力理性酶设计。
4. **文献名称**: "Optimization of BBE1 recombinant protein production in *Pichia pastoris* for industrial applications"
**作者**: Li, R., et al.
**摘要**: 在毕赤酵母系统中优化BBE1重组表达条件，实现高产量和高活性，推动其在药物合成中的规模化应用。
**建议**：实际文献可通过PubMed、Web of Science等平台以“BBE1 recombinant protein”、“berberine bridge enzyme expression”为关键词检索。
The BBE1 (Berberine Bridge Enzyme 1) recombinant protein is a functionally significant enzyme derived from the BBE gene family, originally identified in plants such as *Arabidopsis thaliana* and *Eschscholzia californica* (California poppy). This enzyme plays a critical role in the biosynthesis of benzylisoquinoline alkaloids (BIAs), a class of plant secondary metabolites with pharmacological importance, including morphine, codeine, and berberine. BBE1 catalyzes the oxidative cyclization of (S)-reticuline to (S)-scoulerine, a pivotal step in the BIA pathway, through a unique mechanism involving a covalently bound FAD cofactor.
Recombinant BBE1 is produced via heterologous expression systems, typically in *E. coli* or yeast, enabling large-scale purification for structural and functional studies. Its crystal structure reveals a 45–55 kDa glycoprotein with two distinct domains: an FAD-binding Rossmann fold and a substrate-binding domain. Studies highlight its regioselectivity and stereospecificity, making it a model enzyme for investigating flavoprotein catalysis and alkaloid diversification.
Research on recombinant BBE1 has applications in metabolic engineering for sustainable production of high-value alkaloids and pharmaceutical intermediates. Additionally, it serves as a tool to study plant defense mechanisms, as BIAs contribute to resistance against pathogens and herbivores. Recent advances in protein engineering aim to enhance BBE1’s stability and catalytic efficiency for industrial biocatalysis. Overall, BBE1 recombinant protein bridges plant biochemistry and biotechnological innovation, offering insights into natural product synthesis and therapeutic development.
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