Background:
Excluding humans, the peroxisomal uricase is responsible for the catabolism of uric acid into allantoin in many
species like microorganisms, plants, and invertebrates. Particularly in humans, the synthesis and excretion of uric acid are naturally balanced.
When the uric acid concentration crosses 7 mg/dl will results in conditions such as hyperuricemia and gout. Uricase is one of the potential
source for the reduction of uric acid in humans. Uricase is also widely used as a commercial diagnostic reagent in medical and clinical
biochemistry to estimate the uric acid concentration in blood and other biological fluids. Computational approaches can be used for the
screening and investigation of a uricase enzyme with desirable characteristics that can be employed in diverse industrial applications.
Objectives:
The present study deals with computational-based structural, functional, and phylogenetic analyses of uricase enzymes from
various Bacillus species.
Method:
Seventy uricase protein sequences from Bacillus species were selected for multiple sequence alignment, phylogenetic analysis, motif
assessment, domain architecture examination, understanding of basic physicochemical properties and in silico identification of the
composition of amino acids in uricase. Further, structural (secondary and tertiary structure prediction), and functional (CYS_REC, MOTIF
scan, CD-search, STRING, SOSUI, and PeptideCutter) analysis of uricase were performed.
Results:
Bacillus simplex (WP_063232385.1) was chosen as the representative species of the Bacillus genera. The three-dimensional (3D)
structure of B. simplex uricase is predicted and validated using QMEAN, RAMPAGE, ERRAT, Verify 3D and PROQ servers. Analysis
revealed that the tertiary structure of the selected uricase has good quality and acceptability.
Conclusion:
Computational analysis of uricase from various Bacillus sources revealed that all the selected Bacillus uricases are active within
acidic to a neutral environment, thermally stable with molecular weight ranging from 35.59-59.85kDa. The secondary structure analysis
showed that all uricases are rich in alpha helices and sheets. The CDD tool identified two conserved domains, one of which belongs to OHCU
decarboxylase and another to Uricase superfamily. The quality estimation of 3D modelled protein gave a high overall quality factor score of
94.64. Also, all Bacillus species of uricase enzyme and their corresponding genes showed a strong correlation from the phylogenetic
comparison of the selected taxa. The present detailed computational investigation on the uricase protein could help in screening a suitable
uricase producing microbe with desirable characteristics for industrial application.
