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1.16.99.1
physiological function
enzyme activates methyltrophic corrinoid proteins by reducing cobalt(II) back to cobalt(I). The transfer of electrons to the corrinoid as the electron-accepting site is achieved by increasing the potential of the corrinoid cofactor from -530 mV to -250 mV. The first 50 to 100 mV of the shift of the redox potential are caused by the interaction of nucleotide-bound enzyme with the corrinoid protein or its cofactor. The remaining 1500-200 mV have to be overcome by the chemical energy of ATP hydrolysis
762344
1.16.99.1
physiological function
RamA is required for in vitro ATP-dependent reductive activation of methylamine:CoM methyl transfer from monomethylamine, dimethylamine, or trimethylamine. In the absence of the methyltransferases, RamA mediates the ATP-dependent reductive activation of Co(II) corrinoid to the Co(I) state for the monomethylamine corrinoid protein, MtmC
761440
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