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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Bibliographic Details
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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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2360489