The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii.
The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii.
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谢尔曼丙酸杆菌甲基丙二酰辅酶 A 变位酶的亚基结构。
作者：
F. Francalanci;N. Davis;J. Fuller;D. Murfitt;P. Leadlay
通过简化的程序从谢氏丙酸杆菌中纯化5 '-脱氧腺苷钴胺素依赖性甲基丙二酰辅酶A β。天然酶的表观Mr为165，000，与其他来源的酶相似，但比以前报道的要大。它由两个不同的亚基组成，分别为Mr 79，000和67，000。较小的亚基显然不是较大亚基的蛋白水解片段。最后的制剂通常含有一些无活性的维生素，带有牢固结合的钴胺素种类。这种蛋白质被证明是容易分离的脱辅基酶快速蛋白质液相色谱上的阴离子交换柱。
5'-Deoxyadenosylcobalamin-dependent methylmalonyl-CoA mutase was purified to homogeneity from Propionibacterium shermanii by a simplified procedure. The native enzyme has an apparent Mr of 165,000, similar to the enzyme from other sources but larger than previously reported. It consists of two non-identical subunits, of Mr 79,000 and 67,000 respectively. The smaller subunit is apparently not a proteolytic fragment of the larger one. The final preparation usually contained some inactive mutase, bearing a tenaciously bound cobalamin species. This protein proved to be readily separable from apoenzyme by fast protein liquid chromatography on anion-exchange columns.