纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | fabB |
Uniprot No | P0A953 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-406aa |
氨基酸序列 | MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWG NVKLDTTGLIDRKVVRFMSDASIYAFLSMEQAIADAGLSPEAYQNNPRVG LIAGSGGGSPRFQVFGADAMRGPRGLKAVGPYVVTKAMASGVSACLATPF KIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE FDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVEELEHALARG AHIYAEIVGYGATSDGADMVAPSGEGAVRCMKMAMHGVDTPIDYLNSHGT STPVGDVKELAAIREVFGDKSPAISATKAMTGHSLGAAGVQEAIYSLLML EHGFIAPSINIEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLV MRKLKD |
预测分子量 | 61 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FabB重组蛋白的3-4条参考文献示例(注:部分内容基于假设性文献,实际引用需核实):
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1. **"Functional analysis of recombinant FabB in bacterial fatty acid biosynthesis"**
*Cronan, J.E. & Rock, C.O. (1996)*
摘要:研究通过在大肠杆菌中重组表达FabB蛋白,证实其在催化β-酮脂酰-ACP缩合反应中的关键作用,并揭示其对不饱和脂肪酸合成的必要性。
2. **"Crystal structure of Escherichia coli FabB reveals insights into substrate binding"**
*Zhang, Y. et al. (2008)*
摘要:解析了重组FabB蛋白的晶体结构,阐明其活性位点结构及与酰基载体蛋白(ACP)的相互作用机制,为抗生素靶点设计提供依据。
3. **"Role of recombinant FabB in Pseudomonas aeruginosa fatty acid desaturation"**
*Heath, R.J. & Rock, C.O. (2002)*
摘要:利用重组FabB蛋白进行体外酶活实验,证明其在铜绿假单胞菌中调控膜脂不饱和度及环境适应性中的功能。
4. **"Kinetic characterization of recombinant FabB and its inhibition by thiolactomycin"**
*Marrakchi, H. et al. (2003)*
摘要:通过重组FabB的酶动力学分析,揭示了天然抑制剂硫乳霉素对其活性的竞争性抑制作用,为新型抗菌剂开发奠定基础。
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**注:** 以上文献标题及内容为示例性质,实际研究需参考具体发表论文。建议通过PubMed或Web of Science以关键词“FabB recombinant protein”检索最新文献。
FabB, a key enzyme in bacterial fatty acid biosynthesis, is a β-ketoacyl-ACP synthase I (KASI) that catalyzes the elongation cycle of fatty acids in *Escherichia coli* and other Gram-negative bacteria. It plays a critical role in the Type II fatty acid synthesis (FAS II) pathway by condensing malonyl-ACP with acyl-ACP to form β-ketoacyl-ACP, a rate-limiting step for unsaturated fatty acid production. FabB is particularly essential for synthesizing cis-vaccenic acid, a major component of bacterial membranes, and its activity is tightly regulated under anaerobic conditions or during membrane remodeling.
Recombinant FabB protein is engineered for structural, functional, and drug discovery studies. By cloning the *fabB* gene into expression vectors (e.g., pET systems), researchers produce large quantities of the protein in heterologous hosts like *E. coli*. Purification typically involves affinity chromatography (e.g., His-tag) followed by biochemical characterization. FabB's crystal structure reveals a conserved thioesterase domain and active-site residues (Cys163. His303. and His340), providing insights into substrate binding and catalytic mechanisms.
Interest in FabB stems from its dual role as a metabolic engineering target and potential antibiotic target. In synthetic biology, modulating FabB activity can optimize microbial production of biofuels or oleochemicals. Conversely, since FAS II is absent in humans, FabB inhibitors (e.g., thiolactomycin analogs) are explored as narrow-spectrum antimicrobials to combat multidrug-resistant pathogens. However, functional redundancy with FabF (KASII) and bacterial resistance mechanisms pose challenges, driving studies on FabB’s allosteric regulation and interaction with acyl-ACP substrates. Recent advances in cryo-EM and computational modeling further aid in understanding its dynamics and inhibitor design.
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