| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | cyp102A1 |
| Uniprot No | P14779 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1049aa |
| 氨基酸序列 | MTIKEMPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSSQRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILLPSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIGLCGFNYRFNSFYRDQPHPFITSMVRALDEAMNKLQRANPDDPAYDENKRQFQEDIKVMNDLVDKIIADRKASGEQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFALYFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPTAPAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPERFENPSAIPQHAFKPFGNGQRACIGQQFALHEATLVLGMMLKHFDFEDHTNYELDIKETLTLKPEGFVVKAKSKKIPLGGIPSPSTEQSAKKVRKKAENAHNTPLLVLYGSNMGTAEGTARDLADIAMSKGFAPQVATLDSHAGNLPREGAVLIVTASYNGHPPDNAKQFVDWLDQASADEVKGVRYSVFGCGDKNWATTYQKVPAFIDETLAAKGAENIADRGEADASDDFEGTYEEWREHMWSDVAAYFNLDIENSEDNKSTLSLQFVDSAADMPLAKMHGAFSTNVVASKELQQPGSARSTRHLEIELPKEASYQEGDHLGVIPRNYEGIVNRVTARFGLDASQQIRLEAEEEKLAHLPLAKTVSVEELLQYVELQDPVTRTQLRAMAAKTVCPPHKVELEALLEKQAYKEQVLAKRLTMLELLEKYPACEMKFSEFIALLPSIRPRYYSISSSPRVDEKQASITVSVVSGEAWSGYGEYKGIASNYLAELQEGDTITCFISTPQSEFTLPKDPETPLIMVGPGTGVAPFRGFVQARKQLKEQGQSLGEAHLYFGCRSPHEDYLYQEELENAQSEGIITLHTAFSRMPNQPKTYVQHVMEQDGKKLIELLDQGAHFYICGDGSQMAPAVEATLMKSYADVHQVSEADARLWLQQLEEKGRYAKDVWAG |
| 预测分子量 | 117,7 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CYP102A1(细胞色素P450 BM3)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*Directed evolution of cytochrome P450 BM3 for enhanced catalytic activity and substrate selectivity*
**作者**：Otey, C. R., et al. (2006)
**摘要**：该研究通过定向进化技术对CYP102A1进行突变改造，显著提高了其对非天然底物(如短链脂肪酸和药物分子)的催化活性和选择性。突变体F87A/A328V在体外表现出对多种底物的高效羟化能力，为生物催化应用提供了新工具。
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2. **文献名称**：*Functional expression and characterization of cytochrome P450 102A1 from Bacillus megaterium in Escherichia coli*
**作者**：Warman, A. J., et al. (2012)
**摘要**：研究优化了CYP102A1在大肠杆菌中的重组表达系统，通过密码子优化和血红素辅因子供应策略，成功实现了高活性全酶的可溶性表达。该体系为大规模制备CYP102A1及后续酶工程研究奠定了基础。
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3. **文献名称**：*Structural basis for the fatty acid chain length specificity of cytochrome P450 BM3*
**作者**：Haines, D. C., et al. (2001)
**摘要**：通过X射线晶体学解析了CYP102A1与其天然底物(长链脂肪酸)的结合结构，揭示了F87和A328等关键残基在底物识别中的作用，阐明了其链长选择性的分子机制，为理性设计底物结合口袋提供了依据。
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4. **文献名称**：*Engineering cytochrome P450 BM3 for terminal oxygenation of n-alkanes*
**作者**：Fasan, R., et al. (2007)
**摘要**：通过半理性设计改造CYP102A1的活性中心，使其能够催化正构烷烃的末端羟化反应。突变体T268A/A328F对C8-C12烷烃表现出显著活性，拓展了其在生物燃料合成中的应用潜力。
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以上文献涵盖CYP102A1的定向进化、表达优化、结构机制及工程应用，均为该领域经典研究。
CYP102A1. commonly known as cytochrome P450 BM3 (BM3), is a bacterial monooxygenase originally discovered in *Bacillus megaterium*, a Gram-positive soil bacterium. This enzyme is a natural fusion protein comprising a heme-containing cytochrome P450 domain (responsible for substrate oxidation) and a reductase domain (NADPH-dependent flavoprotein), enabling self-sufficient catalytic activity without requiring external redox partners. First characterized in the 1980s, CYP102A1 naturally catalyzes the hydroxylation of long-chain fatty acids (C12–C20) as part of bacterial secondary metabolism, displaying exceptionally high catalytic turnover rates compared to mammalian P450 enzymes.
Its unique structural and functional properties have made CYP102A1 a model system for studying P450 enzymology and a versatile platform for biotechnological applications. The enzyme's broad substrate promiscuity and high stability under industrial conditions have driven its engineering via directed evolution or rational design to expand its substrate scope beyond fatty acids. Engineered BM3 variants now efficiently oxidize non-native substrates, including pharmaceuticals (e.g., omeprazole, propranolol), aromatic hydrocarbons, and terpenes, enabling their use in drug metabolite synthesis, biosensor development, and environmental pollutant degradation.
Recombinant CYP102A1 is typically expressed in *Escherichia coli* for laboratory and industrial use, benefiting from straightforward genetic manipulation and high-yield production. Its commercial availability and adaptability have positioned it as a key tool in green chemistry, offering a sustainable alternative to traditional chemical synthesis methods. Ongoing research focuses on improving catalytic efficiency, stereoselectivity, and stability under extreme conditions, with applications spanning pharmaceuticals, agrochemicals, and biofuel production. Its structural insights also contribute to understanding human P450 enzymes, aiding drug metabolism studies and toxicity prediction.
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