Purification of methylmalonyl-CoA mutase from Propionibacterium shermanii using affinity chromatography

Murthy, Vadiraja V.; Jones, E T; Cole, Thomas W.; Johnson, J D

doi:10.1016/0005-2744(77)90079-1

Cited by 3 publications

(3 citation statements)

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“…Approx. 4 x 105 plaques of a mouse liver cDNA library in Agtll (Stratagene) were screened and cDNA inserts were subcloned into the vector pGEM7zf(+) (Promega) [19,20]. Both strands of the mouse cDNA were sequenced by using subclones containing internal restriction fragments or terminal deletions introduced by ExollI digestion (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…In prokaryotes such as Propionibacterium shermanii [4], Streptomyces erythreus [5] and Protaminobacter ruber [6] and eukaryotes such as Fasciola hepatica [7] and Spirometra mansonoides [7], MCM catalyses the isomerization of succinyl-CoA to methylmalonyl-CoA during synthesis of propionate from tricarboxylic acid-cycle intermediates.…”

Section: Introductionmentioning

confidence: 99%

“…MCM has been purified from several species, including humans [8,9], Prop. shermanii [4,10], Strep. erythreus [5] and Ascaris lumbricoides [11].…”

Section: Introductionmentioning

confidence: 99%

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Primary structure and activity of mouse methylmalonyl-CoA mutase

Wilkemeyer

Crane

Ledley

1990

Biochemical Journal

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Methylmalonyl-CoA mutase (MCM) is an adenosylcobalamin-dependent enzyme that catalyses isomerization between methylmalonyl-CoA and succinyl-CoA (3-carboxypropionyl-CoA). Genetic deficiency of this enzyme in man causes an often fatal disorder of organic acid metabolism termed mut methylmalonicacidaemia. We report cloning of a mouse MCM cDNA and the characterization of its primary structure and biological function. Mouse MCM in fibroblasts and crude liver extracts exhibits activity and reaction kinetics similar to those of the human enzyme. The predicted amino acid sequence of mouse MCM exhibits 94% identity with its human homologue and considerable identity with a prokaryotic MCM. Transfection of the mouse cDNA into cultured cells constitutes an active apoenzyme and can complement genetic deficiency of the apoenzyme in cells from patients with mut methylmalonicacidaemia. These results establish that mouse MCM is homologous to human MCM in structure and function and provides a basis for using the mouse as a model for studying this enzyme and its deficiency state.

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Section: Methodsmentioning

confidence: 99%