4b10
Plasmodium vivax N-myristoyltransferase with a non-hydrolysable co- factorPlasmodium vivax N-myristoyltransferase with a non-hydrolysable co- factor
Structural highlights
FunctionA5K1A2_PLAVS Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).[RuleBase:RU000586] Publication Abstract from PubMedDesign of inhibitors for N-myristoyltransferase (NMT), an enzyme responsible for protein trafficking in Plasmodium falciparum , the most lethal species of parasites that cause malaria, is described. Chemistry-driven optimization of compound 1 from a focused NMT inhibitor library led to the identification of two early lead compounds 4 and 25, which showed good enzyme and cellular potency and excellent selectivity over human NMT. These molecules provide a valuable starting point for further development. Design and Synthesis of Inhibitors of Plasmodium falciparum N-Myristoyltransferase, A Promising Target for Antimalarial Drug Discovery.,Yu Z, Brannigan JA, Moss DK, Brzozowski AM, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ J Med Chem. 2012 Oct 15. PMID:23035716[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|