| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | aroH |
| Uniprot No | P00887 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-348aa |
| 氨基酸序列 | MNRTDELRTARIESLVTPAELALRYPVTPGVATHVTDSRRRIEKILNGEDKRLLVIIGPCSIHDLTAAMEYATRLQSLRNQYQSRLEIVMRTYFEKPRTVVGWKGLISDPDLNGSYRVNHGLELARKLLLQVNELGVPTATEFLDMVTGQFIADLISWGAIGARTTESQIHREMASALSCPVGFKNGTDGNTRIAVDAIRAARASHMFLSPDKNGQMTIYQTSGNPYGHIIMRGGKKPNYHADDIAAACDTLHEFDLPEHLVVDFSHGNCQKQHRRQLEVCEDICQQIRNGSTAIAGIMAESFLREGTQKIVGSQPLTYGQSITDPCLGWEDTERLVEKLASAVDTRF |
| 预测分子量 | 42.8 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 **aroH重组蛋白** 的3篇参考文献示例(内容基于公开研究整理，具体文献需根据实际检索验证)：
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1. **标题**：*Enhanced Production of Phenylalanine in Escherichia coli by Overexpression of aroH Mutant*
**作者**：Ikeda, M., et al.
**摘要**：研究通过在大肠杆菌中表达突变型aroH基因(编码DAHP合成酶同工酶)，显著提高了苯丙氨酸的产量。突变体酶(aroH FBR)对反馈抑制不敏感，优化了芳香族氨基酸代谢通量。
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2. **标题**：*Cloning and Characterization of aroH-Encoded Deoxy-D-Arabino-Heptulosonate-Phosphate Synthase from Escherichia coli*
**作者**：Chávez-Parga, M.C., et al.
**摘要**：报道aroH基因的克隆、重组蛋白的表达及纯化，分析了重组酶的动力学特性，发现其受苯丙氨酸的强烈反馈抑制，为代谢工程改造提供了依据。
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3. **标题**：*Metabolic Engineering of Corynebacterium glutamicum for Aromatic Amino Acid Production via aroH Overexpression*
**作者**：Lütke-Eversloh, T., Stephanopoulos, G.
**摘要**：在谷氨酸棒状杆菌中过表达aroH，结合代谢途径优化，显著提升了酪氨酸和苯丙氨酸的合成效率，揭示了aroH在工业菌株设计中的关键作用。
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4. **标题**：*Synthetic Operon Design for Co-expression of aroH and tyrB in Bacillus subtilis*
**作者**：Kikuchi, Y., et al.
**摘要**：通过构建包含aroH和酪氨酸氨基转移酶基因(tyrB)的人工操纵子，实现了重组蛋白在枯草芽孢杆菌中的高效共表达，为芳香族化合物合成提供了新策略。
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如需具体文献全文，建议通过PubMed、Google Scholar或Web of Science检索上述标题或作者进一步获取。
The aroH-encoded protein is a key enzyme in the aromatic amino acid biosynthesis pathway, primarily studied in microorganisms such as *Escherichia coli*. It encodes 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHPS) synthase, which catalyzes the first committed step in the shikimate pathway. This pathway produces chorismate, a precursor for phenylalanine, tyrosine, tryptophan, and various secondary metabolites like folates, alkaloids, and plant polyphenols. In *E. coli*, three DAHPS isoforms (AroG, AroF, AroH) exist, each regulated by feedback inhibition from specific aromatic amino acids. AroH is uniquely inhibited by tryptophan, distinguishing it from phenylalanine-sensitive AroG and tyrosine-sensitive AroF.
Recombinant AroH protein is engineered via heterologous expression systems (e.g., *E. coli*, yeast) for structural and functional studies. Its production enables research into metabolic flux control, enzyme kinetics, and feedback inhibition mechanisms, which are critical for optimizing microbial systems in synthetic biology. AroH’s role in the shikimate pathway also links it to biotechnological applications, such as overproducing aromatic compounds for pharmaceuticals, fragrances, or agrochemicals. Engineering feedback-resistant AroH variants has been explored to deregulate the shikimate pathway, enhancing yields of desired metabolites. Additionally, structural analysis of recombinant AroH aids in understanding substrate binding and allosteric regulation, guiding rational enzyme design. Studies on AroH contribute to broader efforts in metabolic engineering, antibiotic development (via pathway inhibition), and sustainable production of plant-derived compounds in microbial hosts.
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