mds 018

PPC-DC, also known as PPCDC, belongs to the HFCD (homo oligomeric flavin containing Cys decarboxylase) superfamily which takes a part in the biosynthesis of coenzyme A (CoA) from pantothenate (Vitamin B). Biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5) is an essential universal pathway in prokaryotes and eukaryotes. This process include several steps: the phosphorylation of pantothenate, the conversion of 4’-hosphopantothenate to 4''-phosphopantetheine, the adenylation by phosphopantetheine adenylyltransferase to form dephospho-CoA and the phosphorylation by dephospho-CoA kinase to form CoA. PPC-DC, one of the last enzymes in this pathway, converts phosphopantothenoylcysteine to 4-prime-phosphopantetheine.

Phosphopantothenoylcysteine Decarboxylase (PPC-DC) is an essential enzyme in the biosynthesis ofCoenzyme A and catalyzes the decarboxylation of PPC to Phosphopantetheine. PPC-DC catalyzes the decarboxylation of the Cysteine moiety of 4-Phosphopantothenoylcysteine (PPC) to form 4-Phosphopantetheine (PPantSH), this reaction forms part of the biosynthesis of Coenzyme A. The enzyme is a member of the larger family of Cysteine Decarboxylases including the Lantibiotic-Biosynthesizing enzymes EpiD and MrsD, all of which use a tightly bound Flavin cofactor to oxidize the Thiol moiety of the substrate to a Thioaldehyde.