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Mechanism of -Adenosyl-l-methionine -Methylation by Cobalamin-dependent Radical -Adenosyl-l-methionine Methylase in 1-Amino-2-methylcyclopropanecarboxylic Acid Biosynthesis. | LitMetric
The radical -adenosyl-l-methionine (SAM) methylase Orf29 catalyzes the -methylation of SAM in the biosynthesis of 1-amino-2-methylcyclopropanecarboxylic acid. Here, we determined that the methylation product is (4″)-4″-methyl-SAM. Furthermore, we found that the 5'-deoxyadenosyl radical generated by Orf29 abstracts the hydrogen atom from the C-4″ position of SAM to generate the radical intermediate, which reacts with methylcobalamin to give (4″)-4″-methyl-SAM. Consequently, the Orf29-catalyzed -methylation was confirmed to proceed with retention of configuration.
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