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S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate = 5'-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate
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methyl-Cob(III)-alamin + CoM = methyl-CoM + Cob(I)-alamin
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methyl-cob(III)alamin + tetrahydrofolate = cob(II)alamin + 5-methyltetrahydrofolate
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5,6,7,8-tetrahydromethanopterin + methylcob(III)alamin = 5-methyl-5,6,7,8-tetrahydromethanopterin + cob(III)alamin
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mercaptopropionate + methylcob(III)alamin = ?
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methyl donor of the reaction
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NMR results support a reaction mechanism in which methylcob(III)alamin is the direct methyl group donor
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the enzyme catalyzes P-methylation using radical S-adenosyl-L-methionine-dependent chemistry with cobalamin as a coenzymemethyl donor of the reaction. The enzyme is active in the absence of methylcobalamin if the strong reductant titanium(III)citrate and hydroxocobalamin are provided
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the enzyme is a radical S-adenosyl-L-methionine enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. According to the proposed mechanism, the reduced iron-sulfur center donates an electron to S-adenosyl-L-methionine, resulting in homolytic cleavage of the carbon-sulfur bond to form a 5'-deoxyadenosyl radical that abstracts the hydrogen atom from the P-H bond of the substrate, forming a phosphinate-centered radical. This radical reacts with methylcob(III)alamin to produce the methylated product and cob(II)alamin, which is reduced by an unknown donor to cob(I)alamin. A potential route for restoring the latter back to methylcob(III)alamin is a nucleophilic attack on a second S-adenosyl-L-methionine molecule
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