Evolutionary and mechanistic insights into substrate and product accommodation of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum (pages 3132–3148)
Gergely N. Nagy, Lívia Marton, Balázs Krámos, Julianna Oláh, Ágnes Révész, Károly Vékey, Frédéric Delsuc, Éva Hunyadi-Gulyás, Katalin F. Medzihradszky, Marina Lavigne, Henri Vial, Rachel Cerdan and Beáta G. Vértessy
Version of Record online: 24 MAY 2013 | DOI: 10.1111/febs.12282
CTP:phosphocholine cytidylyltransferase (CCT) is essential in lipid biosynthesis of Plasmodia, presenting a promising antimalarial target. We identified two independent gene duplication events of CCT within Apicomplexa and characterized a dimeric truncated construct of Plasmodium falciparum CCT. Catalytic mechanism of PfCCT may involve conformational changes affecting the choline subsite of the enzyme whereas Mg2+ cofactor is dispensable for CTP substrate binding.