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. 1986 Jun 1;236(2):489-94.
doi: 10.1042/bj2360489.

The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii

F Francalanci, N K Davis, J Q Fuller, D Murfitt, P F Leadlay

The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii

F Francalanci et al. Biochem J. .

Abstract

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.

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