Journal article
Evolutionary and mechanistic insights into substrate and product accommodation of CTP:phosphocholine cytidylyltransferase from Plasmodium falciparum
Abstract
The enzyme CTP:phosphocholine cytidylyltransferase (CCT) is essential in the lipid biosynthesis of Plasmodia (Haemosporida), presenting a promising antimalarial target. Here, we identified two independent gene duplication events of CCT within Apicomplexa and characterized a truncated construct of Plasmodium falciparum CCT that forms a dimer resembling the molecular architecture of CCT enzymes from other sources. Based on biophysical and enzyme …
Authors
Nagy GN; Marton L; Krámos B; Oláh J; Révész Á; Vékey K; Delsuc F; Hunyadi‐Gulyás É; Medzihradszky KF; Lavigne M
Journal
The FEBS Journal, Vol. 280, No. 13, pp. 3132–3148
Publisher
Wiley
Publication Date
7 2013
DOI
10.1111/febs.12282
ISSN
1742-464X
Associated Experts
Fields of Research (FoR)
Sustainable Development Goals (SDG)
Medical Subject Headings (MeSH)
Amino Acid SequenceApicomplexaBiocatalysisCatalytic DomainCholine-Phosphate CytidylyltransferaseCytidine Diphosphate CholineCytidine TriphosphateDimerizationEnzyme StabilityEvolution, MolecularGene DeletionGene DuplicationMagnesiumModels, MolecularMolecular Sequence DataPhosphorylcholinePlasmodium falciparumProtein BindingProtozoan ProteinsSequence AlignmentSequence Homology, Amino AcidTryptophan