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 C(beta) of the cysteine moiety of 2 is removed during a reversible oxidation of the thiol to a thioaldehyde intermediate.
Strauss
Erick
E
Department of Chemistry and Chemical Biology, Cornell University, Baker Laboratory, Ithaca, NY 14853, USA.
Begley
Tadhg P
TP
D001665:Binding Sites; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000302:isolation & purification; D003065:Coenzyme A / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013237:Stereoisomerism
D002262:Carboxy-Lyases; C022373:Phosphopantothenoyl-cysteine decarboxylase; D003065:Coenzyme A