Characterization of a three-component vanillate O-demethylase from Moorella thermoacetica

The Moorella thermoacetica aromatic O-demethylase was characterized as an i nducible three-component system with similarity to the methanogenic methano l, methylamine, and methanethiol methyltransferases and to the O-demethylas e system from Acetobacterium dehalogenans. MtvB catalyzes methyl transfer f rom a phenylmethylether to the cobalt center of MtvC, a corrinoid protein. MtvA catalyzes transmethylation from MtvC to tetrahydrofolate, forming meth yltetrahydrofolate. Cobalamin can substitute for MtvC.