Nieto CA, Marín CY, Contreras LE and Ramírez MH
Nicotinamide mononucleotide adenylyl transferase (NMNAT) is a key enzyme in the biosynthesis of nicotinamide adenine dinucleotide (NAD+), which is an essential molecule in cellular metabolism. Specific sequences have been described in other NMNATs, which are associated with the regulation of catalytic activity and intracellular localization. In addition, it has been observed that prokaryotic NMNATs have specific regions that could be used as possible therapeutic targets. By aligning Plasmodium falciparum (Pf) NMNAT sequences with their human orthologues (HsNMNAT), specific domains of the P. falciparum protein can be observed. PfNMNAT mutants were designed using bioinformatics software to obtain 2 mutants in order to evaluate the specific sequences of the P. falciparum enzyme. For mutant construction, t-directed mutagenesis was used to introduce changes in the wild-type maltose binding protein (MBP)-PfNMNAT clone previously obtained. The results were compared to those obtained with the wild-type protein. The experimental evidence indicates that the catalytic activity of the enzyme can be affected by transitional and transversional amino acid changes in charge and size. The study of these mutants allows an approach to studying the function and regulation of these proteins.
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