Article
Dedicated metallochaperone connects apoenzyme and molybdenum cofactor biosynthesis components.
The Journal of biological chemistry - 1 Aug 2008
Genest Olivier, Neumann Meina, Seduk Farida, Stöcklein Walter, Méjean Vincent, Leimkühler Silke, Iobbi-Nivol Chantal
Abstract excerpt
The biogenesis of molybdenum-containing enzymes is a sophisticated process involving the insertion of a complex molybdenum cofactor into competent apoproteins. As for many molybdoenzymes, the maturation of trimethylamine-oxide reductase TorA requires a private chaperone. This chaperone (TorD) interacts with the signal peptide and the core of apo-TorA. Using random mutagenesis, we established that alpha-helix 5 of...
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