Stereochemical studies on phosphopantothenoylcysteine decarboxylase from Escherichia coli

Phosphopantothenoylcysteine decarboxylase catalyzes the decarboxylation of 4′-phosphopantothenoylcysteine (2) to form 4′-phosphopanthetheine (3), an intermediate in the biosynthesis of Coenzyme A. In this study we investigated the stereochemistry of this reaction. Our results show that the decarboxylation proceeds with retention of stereochemistry, and that the pro-R proton at Cβ of the cysteine moiety of 2 is removed during a reversible oxidation of the thiol to a thioaldehyde intermediate.