In Silico analysis and homology modelling of carbohydrate metabolic enzymes from Corynebacterium Pseudotuberculosis Available to Purchase

Corynebacterium pseudotuberculosis is responsible for caseous lymphadenitis in ruminants that contribute to significant economic loss to many countries. A wide range of studies has been carried out to understand the molecular biology of this pathogen, develop the diagnostic tools and improve the therapeutic strategies. However, little is known about the carbohydrate metabolism in C. pseudotuberculosis. The structure and function of C. pseudotuberculosis enzymes associated with the carbohydrate metabolism remain not well investigated. Therefore, the present study was performed to develop 3D structural model of carbohydrate metabolic enzymes from C. pseudotuberculosis. Herein, the physicochemical properties of 1-phosphofructokinase, triosephosphate isomerase, L-lactate dehydrogenase, enolase and phosphoglucosamine mutase were computed using ProtParam from ExPASy server. Meanwhile, the PSIPRED version 4.0 was used to predict the secondary structure of enzymes. Homology modelling of enzymes was performed using SWISS-MODEL while the quality of 3D enzyme models was evaluated using Ramachandran plot. Results demonstrated that all the enzymes were predicted to be stable in a test tube (Instability index < 40) and possess high thermostability (Aliphatic index > 80). The enzymes were also predicted to be rich in alpha helix secondary structural motif. All the 3D enzyme models showed more than 90% of the residues in most favoured region of the Ramachandran plot. In conclusion, the present study may provide new insights towards understanding the 3D structural conformation of carbohydrate metabolic enzymes from C. pseudotuberculosis, thus providing a basis for the future development of therapeutic strategies against caseous lymphadenitis.