A Comparative Computational analysis of Amino Acid Sequences and Biochemical Properties of Peroxidase Enzymes in Plants, Yeast, Bacteria, and Humans

เปรียบเทียบลำดับกรดอะมิโน และคุณสมบัติทางชีวเคมีของเอนไซม์เพอร์ออกซิเดสในพืช ยีสต์ แบคทีเรีย และมนุษย์

Authors

  • Patsarawadee Paojinda Medical Technology Program, Faculty of Science and Technology, Bansomdejchaopraya Rajabhat University
  • Napat Pimsiri Medical Technology Program, Faculty of Science and Technology, Bansomdejchaopraya Rajabhat University
  • Nunthawadee Niamnuy Medical Technology Program, Faculty of Science and Technology, Bansomdejchaopraya Rajabhat University
  • Piya Wongyanin Medical Technology Program, Faculty of Science and Technology, Bansomdejchaopraya Rajabhat University
  • Pramoon Arooncharus Medical Technology Program, Faculty of Science and Technology, Bansomdejchaopraya Rajabhat University
  • Nittiya Chowchaikong Faculty of Medical Technology, Rangsit University
  • Ranida Tuanudom Preclinic Health Science Center, Faculty of Medicine, Bangkokthonburi University
  • Waranya Imprasittichai Department of Basic Medical Science, Faculty of Medicine Vajira hospital, Navamindradhiraj University

Keywords:

peroxidase , amino acid sequences , bioinformatics

Abstract

          Peroxidases (E.C.1.11.1.7) are commonly found in natural oxidoreductases and can oxidize with various reactants such as guaiacol, pyrogallol, etc. It is popular for use in immunology research, as well as the treatment of phenolic compounds in wastewater, peroxides elimination from raw materials in the food industry, and as biosensor. The objectives of this research were to compare the amino acid sequences and biochemical properties of peroxidase in plants, yeast, bacteria and humans in 7 types including Arabidopsis thaliana, Armoracia rusticana, Escherichia coli, Glycine max, Homo sapiens, Ipomoea batatas, and Saccharomyces cerevisiae from the NCBI database (http://www.ncbi.nlm.nih.gov/protein). The software of the ExPASy SIB Bioinformatics SOPMA tool was used to analyze the physicochemical data by comparing similarities among protein chains, while the ClustalW software was used to analyze the phylogenetic relationships. The lengths of amino acid sequences for peroxidase in plants, yeast, bacteria, and humans were found to be in the ranges of 58 – 352, theoretical pI 4.72-8.76, negative charge (Asp + Glu) 2-45, positive charge (Arg + Lys) 3-32, extinction coefficient 8980-32680, instability index 26.05-59.62, and grand average of hydropathicity (GRAVY)  -0.442-0.190. In the comparison of amino acid sequences for peroxidase among Armoracia rusticana, Arabidopsis thaliana, Escherichia coli, Glycine max, Homo sapiens, Ipomoea batatas, and Saccharomyces cerevisiae, the highest percent identity was found in Arabidopsis thaliana at 65.70%. In the analysis of the phylogenetic relationships, short phylogenetic branches were found in 4 living things including Armoracia rusticana, Arabidopsis thaliana, Glycine max, and Ipomoea batatas, indicating close phylogenetic relationships. The results from this study provide insight into the role of peroxidase in the development of enzymatic engineering to promote the potential of industry, medicine, and bioremediation.

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Additional Files

Published

07-08-2023

How to Cite

1.
Paojinda P, Pimsiri N, Niamnuy N, Wongyanin P, Arooncharus P, Chowchaikong N, Tuanudom R, Imprasittichai W. A Comparative Computational analysis of Amino Acid Sequences and Biochemical Properties of Peroxidase Enzymes in Plants, Yeast, Bacteria, and Humans : เปรียบเทียบลำดับกรดอะมิโน และคุณสมบัติทางชีวเคมีของเอนไซม์เพอร์ออกซิเดสในพืช ยีสต์ แบคทีเรีย และมนุษย์. AdvSciJ [Internet]. 2023 Aug. 7 [cited 2024 Apr. 18];23(2):R125-R142. Available from: https://li02.tci-thaijo.org/index.php/adscij/article/view/508

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Research Articles