Dephospho-coenzyme A kinase (DPCK)

Dephospho-coenzyme A kinase (DPCK; EC 2.7.1.24) is an enzyme that catalyzes the final phosphorylation step in coenzyme A (CoA) biosynthesis, converting dephospho-coenzyme A to coenzyme A by transferring a phosphate from ATP to the 3′-hydroxyl group of the ribose moiety on dephospho-CoA[4][2][5][1]. This enzyme is present in all domains of life, though with structural and sequence diversity between bacteria, eukaryotes, and archaea. In bacteria and lower eukaryotes, it exists as a stand-alone protein, whereas in mammals, it is typically part of a bifunctional coenzyme A synthase along with phosphopantetheine adenylyltransferase activity[2][5]. Its structure includes a canonical nucleotide-binding (P-loop) domain and specific binding sites for both ATP and dephospho-CoA[1][6]. DPCK is considered essential for the survival of various pathogenic organisms and represents a promising but underexplored therapeutic target for anti-infective drug design, provided selective inhibition can be achieved[9][5][6].

Other names

Dephosphocoenzyme A kinase3′-dephospho-CoA kinaseATP:dephospho-CoA 3′-phosphotransferase

Competitive inhibition (e.g., compound A-15 competes with dephospho-CoA for the substrate-binding site in PfDPCK) and non-competitive/uncompetitive inhibition (e.g., compound A-127) have been observed.