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Computational Analysis of Therapeutic Enzyme Uricase from Different Source Organisms
Current Proteomics ( IF 0.5 ) Pub Date : 2020-01-31 , DOI: 10.2174/1570164616666190617165107
Anand Kumar Nelapati 1 , JagadeeshBabu PonnanEttiyappan 1
Affiliation  

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.



中文翻译:

不同来源生物体治疗性尿酸酶的计算分析

背景:高尿酸血症和痛风是这种情况,是血液和尿液中尿酸积累的反应。尿酸是人类嘌呤代谢途径的产物。尿酸酶是一种治疗性酶,可以通过酶法将血清和尿液中的尿酸浓度降低为更多的可溶性尿囊素。尿素酶可通过多种来源广泛获得,例如细菌,真菌,酵母,植物和动物。

目的:本研究旨在通过insilico分析阐明尿酸酶的结构和理化性质。

方法:从NCBI以及不同分析(如多序列比对(MSA),同源性搜索,系统发育关系,基序搜索,结构域结构和包括pI,EC,艾,艾,和被执行。

结果:基于保守氨基酸残基的位置特异性存在,所有选定蛋白质序列的多序列比对在细菌,真菌,植物和动物来源之间均表现出明显差异。所有选定蛋白质序列的最大同源性在51-388之间。在单数类别中,细菌尿酸酶的同源性在16-337之间,真菌尿酸酶的同源性在14-339之间,植物尿酸酶的同源性在12-317之间,动物尿酸酶的同源性在37-361之间。基于公开的氨基酸序列构建的系统树聚类表明尿酸酶来自不同来源。生理化学特征表明,尿酸酶氨基酸残基在300-338之间,分子量为33-39kDa,理论pI范围为4.95-8.88。

结论:在生物信息学领域,这项工作可能是有益的,也是其他研究者了解尿酸酶理化特性,进化史和结构基序的垫脚石,尿酸酶可广泛应用于生物技术和制药行业。因此,建议的计算机分析可以考虑用于蛋白质工程工作以及痛风疗法。

更新日期:2020-01-31
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