| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MMUT |
| Uniprot No | P22033 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-750aa |
| 氨基酸序列 | LHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV |
| 预测分子量 | 84.8 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MMUT(甲基丙二酰辅酶突变酶)重组蛋白的3篇代表性文献摘要示例：
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1. **文献名称**: *Expression and purification of recombinant human methylmalonyl-CoA mutase for functional studies*
**作者**: Smith J, et al.
**摘要**: 本研究报道了人源MMUT在大肠杆菌中的重组表达与纯化。通过优化诱导条件及辅酶维生素B12的添加，获得高活性酶，为体外酶动力学及代谢疾病相关突变分析提供基础。
2. **文献名称**: *Crystal structure of Methylmalonyl-CoA mutase from Pseudomonas aeruginosa*
**作者**: Chen L, et al.
**摘要**: 解析了铜绿假单胞菌来源的MMUT重组蛋白的晶体结构(2.1Å分辨率)，揭示了其底物结合域及催化机制，为设计针对遗传性甲基丙二酸尿症的治疗策略提供结构依据。
3. **文献名称**: *Functional characterization of MMUT mutations using recombinant enzyme assays*
**作者**: Gonzalez R, et al.
**摘要**: 通过构建多种MMUT突变体重组蛋白，检测其酶活性和热稳定性，发现特定突变导致辅酶结合能力下降，解释了临床患者代谢异常的分子机制。
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注：以上文献为示例性质，实际研究需根据具体数据库检索结果调整。建议通过PubMed或Web of Science以关键词“methylmalonyl-CoA mutase recombinant”查找最新文献。
Methylmalonyl-CoA mutase (MMUT), also known as MCM, is a mitochondrial enzyme critical in human metabolism, catalyzing the isomerization of methylmalonyl-CoA to succinyl-CoA—a key step in the catabolism of branched-chain amino acids, odd-chain fatty acids, and cholesterol derivatives. This adenosylcobalamin (vitamin B12)-dependent enzyme plays a vital role in energy production and intermediary metabolism. Genetic mutations in the *MMUT* gene cause methylmalonic acidemia (MMA), a rare inborn error of metabolism characterized by toxic accumulation of methylmalonic acid, leading to metabolic crises, neurological impairment, and multi-organ dysfunction.
Recombinant MMUT protein is engineered to study the molecular mechanisms of MMA and develop therapeutic strategies. Produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), the recombinant protein retains enzymatic activity when complexed with its cofactor B12. Its production enables structural analysis (e.g., X-ray crystallography) to map mutation-induced conformational changes, aiding in understanding genotype-phenotype correlations. Additionally, recombinant MMUT serves as a tool for high-throughput drug screening to identify chaperones or stabilizers that rescue enzyme function in pathogenic variants. Recent advances explore its potential in enzyme replacement therapy (ERT) or gene therapy, though challenges like mitochondrial targeting and immunogenicity remain. Beyond clinical applications, it is utilized in industrial biocatalysis for stereospecific chemical synthesis. Research continues to optimize expression yield, stability, and functional fidelity of recombinant MMUT to bridge gaps between biochemical insights and therapeutic translation.
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