Phosphopantothenoylcysteine decarboxylase (PPCDC)

Phosphopantothenoylcysteine decarboxylase (PPCDC, also known as CoaC) is an essential enzyme in the biosynthesis of coenzyme A (CoA), a vital cofactor in numerous metabolic reactions. PPCDC catalyzes the decarboxylation of 4'-phosphopantothenoylcysteine to form 4'-phosphopantetheine, which is the immediate precursor of CoA[1][2]. In most eukaryotes, including humans, PPCDC functions as a homotrimer, with each active site formed at the interface of adjacent monomers. The enzyme requires two catalytically essential residues—a histidine for oxidative decarboxylation and a cysteine for reduction of the enethiol intermediate—each donated by a different protomer in the trimer[1]. In yeast, PPCDC activity results from a heterotrimeric complex between Hal3, Vhs3, and Cab3, with each contributing a different active-site residue, reflecting a unique evolutionary adaptation[1]. In humans, PPCDC is a single polypeptide chain, and its disruption would impair CoA biosynthesis, with expected broad metabolic consequences, though specific disease associations are not well documented in the literature[1][2]. There is currently no direct evidence of PPCDC being targeted by clinically approved drugs, and no known interacting drugs, biomarkers, or notable safety concerns have been reported.

Other names

CoaCMDS018UNQ9365/PRO34154PPC-DCFLJ14585coaCPhosphopantothenoylcysteine decarboxylasePPCDC