[01] Nahla O. M. Ali, Department of Parasitology, Faculty of Veterinary Medicine, University of Khartoum, Khartoum, Sudan.

In this study, PGM2 enzyme from different malaria parasite Plasmodium species was analyzed and presented in this communication. The composition of leucine, lysine and asparagines were the highest while lowest concentrations of tryptophan and histidine residues were noticed when compared to other amino acids. The pI value of P. vinckei PGM2 was 8.59 while the lowest pI of 5.91 was shown by P. vivax PGM2. The instability index of all the enzymes is variable, but for all of them it was less than 40, which indicates that all of them are stable. The aliphatic index was found to span within a range of 83 to 86. Secondary structural analysis of the enzymes showed the pre-dominance of Alpha helix followed by random coils for all the mutases except P. vivax, P. inui, P. Knowlesi and P. Fragile PGM2 enzyme. The significance of the above results is discussed in the light of existing literature.

PGM2, Phosphoglucomutase, Plasmodium spp., Bioinformatics, Secondary Structure

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