The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii.
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.
D000596:Amino Acids / Q000032:analysis; D002852:Chromatography, Ion Exchange; D003038:Cobamides / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D007535:Isomerases / Q000302:isolation & purification*; D008765:Methylmalonyl-CoA Mutase / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011424:Propionibacterium / Q000201:enzymology*
D000596:Amino Acids; D003038:Cobamides; D010446:Peptide Fragments; D007535:Isomerases; D008765:Methylmalonyl-CoA Mutase; C000913:cobamamide