Urease, an important plant enzyme, specifically with reference to foliar urea hydrolysis, was explored in the present study. An in-silico analysis was conducted to investigate the structural and functional properties of urease in wheat (Triticum aestivum L.), and its interaction with urea. This will help explore the enzyme and its catalytic activity. Further, considering the limited literature on the study of cereal urease, this is the first and foremost in-silico report for wheat urease and its interaction with urea. Initially, the 3-D structure of wheat urease was predicted through homology modelling, validated and found to be a homotrimer. Docking with urea reported a binding energy of − 4.1 kcal mol− 1. Alanine, histidine, glycine and aspartate were found to be involved in the substrate binding. The molecular dynamic (MD) simulation studies, including root mean square deviation (RMSD), root mean square fluctuation (RMSF), radius of gyration (Rg) and solvent accessible surface area (SASA), depicted the stability of the protein-ligand complex. The Rg and SASA values for urease were continuously stable throughout the simulations, with values of 3.075 nm and 350 nm2, respectively, indicating the enzyme’s stability during simulations. A thorough understanding of urease’s role in wheat urea metabolism delved into its importance for cereal crops following foliar urea application, and a contribution towards sustainable agriculture.
Sahewalla et al. (Thu,) studied this question.
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