EC Number   |
General Information |
Reference |
|---|
    2.7.1.24 | evolution |
all the eukaryotic-type enzymes of CoA de novo biosynthesis pathway are conserved in all Plasmodium species. Unlike mammalian cells and similar to bacteria, the PPAT and DPCK enzymes are encoded on two different genes and not on one gene that encodes a bifunctional protein |
759223 |
| 2.7.1.24 | evolution |
enzyme DPCK, encoded by the TK1697 gene of Thermococcus kodakarensis is not homologous to the classical DPCK from bacteria and eukaryotes but is distantly related to bacterial and eukaryotic thiamine diphosphokinases. Orthologues of TK1697 are widely distributed in archaea, suggesting that this form of DPCK is responsible for the last step of CoA biosynthesis in most of the archaea |
-, 759707 |
| 2.7.1.24 | malfunction |
disruption of the TK1697 results in CoA auxotrophy |
-, 759707 |
| 2.7.1.24 | metabolism |
conservation of CoA biosynthesis pathway in all malaria parasite species. A schematic representation of the canonical biosynthesis pathway of CoA from pantothenate with enzymes PanK (pantothenate kinase), PPCS (phosphopantothenylcysteine synthase), PPCDC (phosphopantothenylcysteine decarboxylase), PPAT (phosphopantetheine adenylyltransferase), and DPCK (dephospho-CoA kinase), respectively. In contrast to the first two enzymes of this pathway, the last two enzymes for CoA biosynthesis are essential for blood stage parasites |
759223 |
| 2.7.1.24 | metabolism |
the enzyme DCPK catalyzes the final step in the biosynthesis of CoA |
758838 |
| 2.7.1.24 | metabolism |
the pathway for CoA biosynthesis in archaea compared to those of plants and bacteria, overview |
-, 759707 |
| 2.7.1.24 | more |
intracellular metabolite extraction of wild-type expressing and silenced-mutant strain. DPCKs comprise three domains: the nucleotide-binding domain in parallel beta-sheet, the substrate-binding domain in alpha-helices, and the LID domain. All of these DPCK features are present in EhDPCK. Isozymes EhDPCK1 and 2 show striking similarity based on three-dimensional structure predicted by homology modeling, structural comparison of EhDPCK and its mammalian counterpart from mouse, overview |
759246 |
| 2.7.1.24 | physiological function |
in the cytosol, the monofunctional DPCK transforms dephospho-CoA to CoA |
758838 |
| 2.7.1.24 | physiological function |
the enzyme is involved in biosynthesis of CoA, an essential cofactor for all prokaryotes and eukaryotes to support a large number of metabolic processes including fatty acid biosynthesis and oxidation, as well as carbohydrate and amino acid metabolism. PPAT (phosphopantetheine adenylyltransferase), and DPCK (dephospho-CoA kinase) are essential for growth of blood stage parasites |
759223 |
| 2.7.1.24 | physiological function |
TK1697 gene-encoded DPCK contributes to CoA biosynthesis in Thermococcus kodakarensis. CoA is utilized in a wide range of metabolic pathways, and its biosynthesis is essential for life |
-, 759707 |
