Structural highlights
Function
Q4Q5S8_LEIMA Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).
Publication Abstract from PubMed
The parasite Plasmodium vivax is the most widely distributed cause of recurring malaria. N-Myristoyltransferase (NMT), an enzyme that catalyses the covalent attachment of myristate to the N-terminal glycine of substrate proteins, has been described as a potential target for the treatment of this disease. Herein, we report the synthesis and the structure-guided optimization of a series of quinolines with balanced activity against both Plasmodium vivax and Plasmodium falciparum N-myristoyltransferase (NMT).
Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase.,Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11. PMID:28626547[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goncalves V, Brannigan JA, Laporte A, Bell AS, Roberts SM, Wilkinson AJ, Leatherbarrow RJ, Tate EW. Structure-guided optimization of quinoline inhibitors of Plasmodium N-myristoyltransferase. Medchemcomm. 2017 Jan 1;8(1):191-197. doi: 10.1039/c6md00531d. Epub 2016 Nov 11. PMID:28626547 doi:http://dx.doi.org/10.1039/c6md00531d
