Methylmalonyl-CoA mutase from Propionibacterium shermanii: characterization of the cobalamin-inhibited form and subunit-cofactor interactions studied by analytical ultracentrifugation.

A large proportion of adenosylcobalamin-dependent methylmalonyl-CoA mutase from Propionibacterium shermannii is isolated in an inactive form which contains a tightly bound cobalamin. Even when the enzyme was denatured in 5.0 M guanidine hydrochloride the cobalamin remained associated with the protei...

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Sparad:
Bibliografiska uppgifter
Huvudupphovsmän: Marsh, E N, Harding, S E
Materialtyp: Artigo
Språk:Inglês
Publicerad: 1993
Ämnen:
Research Article
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC1132309/
https://ncbi.nlm.nih.gov/pubmed/8095783
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