Structural and Functional Insights into Fungal Uricases: A Computational Approach

Gout is a prevalent rheumatic disorder arising from elevated uric acid levels in the bloodstream, a condition known as hyperuricemia. Uricase serves the purpose of reducing uric acid levels nevertheless, it is absent in humans as a result of evolutionary modifications. The present investigation focused on the computational analysis of uricase enzymes derived from eighty-eight fungal species and the analysis includes their structural, functional, physicochemical properties, motif search and domain architecture analysis were done. In addition to this we have performed the phylogenetic analysis of these protein sequences to study their phylogenetic relationship. Physicochemical analysis revealed that uricase spans amino acid residues 296-330, with a molecular weight of 33.03-35.05 kDa and theoretical pI values of 5.71 to 9.03. Valine was the most prevalent amino acid, averaging 8.40% across all species. These uricase were thermally stable and active in acidic and alkaline conditions. The secondary structure analysis indicated a predominance of alpha-helices and beta-sheets in uricase. Aspergillus niger (ABI79319.1) was chosen as the representative species, with its three-dimensional structure accurately predicted and validated. The comprehensive computational analysis conducted on the uricase protein offers the potential to identify a suitable microorganism capable of producing uricase with desirable characteristics for industrial applications.