Abstract
2-Amino-2-methylmalonic acid and both of its [1-13C]-enantiomers were synthesised and were used to probe the stereochemical course of the aminomalonic acid decarboxylation reaction catalysed by serine hydroxymethyltransferase. The decarboxylation reaction is stereospecific, contrary to previous findings, and occurs via cleavage of the pro-R carboxyl group of 2-amino-2-methylmalonic acid. The carboxyl group was replaced by a proton with retention of configuration at C-2, to give exclusively (2R)-alanine. The stereochemical course for the decarboxylation reaction parallels that of the physiologically important aldolase reaction.
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