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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...

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Published in:	Biochemical journal 1986-06, Vol.236 (2), p.489-494
Main Authors:	Francalanci, F, Davis, N K, Fuller, J Q, Murfitt, D, Leadlay, P F
Format:	Article
Language:	English
Subjects:	Amino Acids - analysis anion-exchange chromatography Chromatography, Ion Exchange Cobamides - pharmacology Electrophoresis, Polyacrylamide Gel Isomerases - isolation & purification liquid chromatography methylmalonyl-CoA mutase Methylmalonyl-CoA Mutase - isolation & purification Methylmalonyl-CoA Mutase - metabolism Molecular Weight Peptide Fragments - analysis Propionibacterium - enzymology Propionibacterium shermanii subunit structure
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container_issue	2
container_start_page	489
container_title	Biochemical journal
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creator	Francalanci, F Davis, N K Fuller, J Q Murfitt, D Leadlay, P F
description	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.
doi_str_mv	10.1042/bj2360489
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language	eng
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subjects	Amino Acids - analysis anion-exchange chromatography Chromatography, Ion Exchange Cobamides - pharmacology Electrophoresis, Polyacrylamide Gel Isomerases - isolation & purification liquid chromatography methylmalonyl-CoA mutase Methylmalonyl-CoA Mutase - isolation & purification Methylmalonyl-CoA Mutase - metabolism Molecular Weight Peptide Fragments - analysis Propionibacterium - enzymology Propionibacterium shermanii subunit structure
title	The subunit structure of methylmalonyl-CoA mutase from Propionibacterium shermanii
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