Stereochemistry of Decarboxylation Reactions Catalyzed by a Constitutive Aromaticl-Amino Acid Decarboxylase

Abstract
The stereochemistry of the decarboxylation reaction catalyzed by an aromatic l-amino acid decarboxylase, purified from Micrococcus percitreus, was studied using stereospecifically deuterium labelled phenylalanine (Phe). The 1H NMR spectrum of [1,2-2H2]-β-phenethylamine enzymatically derived from (2S, 3R)-[3-2H]-Phe in 2H2O was compared with that of [1-2H]-β-phenethylamine from unlabelled Phe in 2H2O. The results clearly indicate that the decarboxylation reaction of this enzyme proceeds exclusively through a course in which the configuration at C-2 of Phe is retained.

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