Homology Modeling of Phosphoenolpyruvate Carboxykinase of Ascaris suum

Phosphoenolpyruvate carboxykinase (PEPCK) is present in parasites as well as in their mammalian hosts it serves different functions. In the host PEPCK catalyses the reaction from oxaloacetate to make phosphoenol pyruvate and carbon dioxide, part of the gluconeogenesis pathway. Parasite PEPCK catalyses the reverse reaction to form oxaloacetate, the precursor of malate, which is metabolized anaerobically by the mitochondria. This functional difference is related to significant differences in the molecular properties of the parasite PEPCK. These differences between the mammalian and the parasite enzyme support the belief that PEPCK should be further investigated as a possible target for selective chemotherapeutic agents. The 3D structure of PEPCK of any helminthes group is not available in protein data bank. Therefore, based on the knowledge of the template, a three-dimensional model of PEPCK of Ascaris suum was predicted using Modeller 9 v 10 software and processed in to energy minimization, Ramachandran plot analysis, quality assessment and finally deposited into Protein Model Database. Infections with parasitic helminthes are important causes of morbidity and mortality worldwide. New drugs that are parasite specific and minimally toxic to the host are needed to counter these infections effectively. Therefore, the present study will help to target this enzyme for further development of new antihelminthic drugs.