Title:Computational Analysis of Therapeutic Enzyme Uricase from Different Source Organisms
VOLUME: 17 ISSUE: 1
Author(s):Anand Kumar Nelapati and JagadeeshBabu PonnanEttiyappan*
Affiliation:Department of Chemical Engineering, National Institute of Technology Karnataka, Srinivasanagar, Surathkal, Mangalore 575025, Karnataka, Department of Chemical Engineering, National Institute of Technology Karnataka, Srinivasanagar, Surathkal, Mangalore 575025, Karnataka
Keywords:Uricase, homology, MSA, phylogenetic tree, motifs, domains, physicochemical properties.
Abstract:Background: Hyperuricemia and gout are the conditions, which is a response of accumulation
of uric acid in the blood and urine. Uric acid is the product of purine metabolic pathway in humans.
Uricase is a therapeutic enzyme that can enzymatically reduces the concentration of uric acid in
serum and urine into more a soluble allantoin. Uricases are widely available in several sources like
bacteria, fungi, yeast, plants and animals.
Objective: The present study is aimed at elucidating the structure and physiochemical properties of
uricase by insilico analysis.
Methods: A total number of sixty amino acid sequences of uricase belongs to different sources were
obtained from NCBI and different analysis like Multiple Sequence Alignment (MSA), homology
search, phylogenetic relation, motif search, domain architecture and physiochemical properties including
pI, EC, Ai, Ii, and were performed.
Results: Multiple sequence alignment of all the selected protein sequences has exhibited distinct difference
between bacterial, fungal, plant and animal sources based on the position-specific existence of
conserved amino acid residues. The maximum homology of all the selected protein sequences is
between 51-388. In singular category, homology is between 16-337 for bacterial uricase, 14-339 for
fungal uricase, 12-317 for plants uricase, and 37-361 for animals uricase. The phylogenetic tree constructed
based on the amino acid sequences disclosed clusters indicating that uricase is from different
source. The physiochemical features revealed that the uricase amino acid residues are in between 300-
338 with a molecular weight as 33-39kDa and theoretical pI ranging from 4.95-8.88. The amino acid
composition results showed that valine amino acid has a high average frequency of 8.79 percentage
compared to different amino acids in all analyzed species.
Conclusion: In the area of bioinformatics field, this work might be informative and a stepping-stone to
other researchers to get an idea about the physicochemical features, evolutionary history and structural
motifs of uricase that can be widely used in biotechnological and pharmaceutical industries. Therefore,
the proposed in silico analysis can be considered for protein engineering work, as well as for gout therapy.