In- silico Analysis of Manganese Peroxidases from Different Fungal Sources

Title:In- silico Analysis of Manganese Peroxidases from Different Fungal Sources

Volume: 14 Issue: 3

Author(s): Meera Yadav*, Sangeeta Yadav, Dinesh Yadav and KDS Yadav

Affiliation:

• Dept of Chemistry, NERIST, Nirjuli, Itanagar-791109 (A.P),India

Keywords: Manganese peroxidases, homology search, motifs, phylogenetic tree, in-silico, fungal sources.

Abstract: Background: The relevance of bioinformatics is being realized in the era of genomics, assisting in genome-wide identification and characterization of putative gene families of different enzymes for diverse industrial applications. Therefore, in the present manuscript, Mn peroxidases protein sequences from different fungal sources were subjected to bioinformatics assessment for homology search, multiple sequence alignment, phylogenetic tree construction and motif search.

Objectives: The available protein sequences representing enzymes is being utilized to decipher the sequence-structure-functional relationship with the aid of bioinformatics tools. In-silico analysis of protein sequences of several industrially important enzymes with an aim to improve the catalytic efficiency, thermostability, structural prediction and validation have been reported in recent years.

Method: A total of 78 full length protein sequences representing manganese peroxidases from diverse fungal sources have been retrieved from GenBank and subjected to in-silico analysis for homology search, physio-chemical attributes, multiple sequence alignment, phylogenetic tree and motif assessments. Multiple accessions from same fungal sources like 9 accessions of Puncularia strigoso zonata were included to get an insight into the structural and functional diversity of the Mn Peroxidases.

Results: The physio-chemical attributes showed variability in the amino acid residues ranging from 341 to 613, molecular weight from 31939.035 to 58082.9 daltons while the pI ranging from 3.8 to 5.39. Thermostability and hydrophilic nature of these proteins was predominantly observed as revealed by comparatively high value of aliphatic index and negative value of GRAVY respectively. The phylogenetic tree revealed distinct clusters for different fungal genus and multiple accessions representing the same genus were grouped together indicating sequence level similarity.

Conclusion: Five motifs were uniformly observed among all the sequences and these revealed similarities to Plant_ peroxidase_family. The plant peroxidase-like superfamily is reported to be prevalent in three kingdoms of life and know to carry out a variety of biosynthetic and degradative functions.

Cite this article as:

Yadav Meera *, Yadav Sangeeta , Yadav Dinesh and Yadav KDS , In- silico Analysis of Manganese Peroxidases from Different Fungal Sources, Current Proteomics 2017; 14 (3) . https://dx.doi.org/10.2174/1570164614666170203165022

DOI https://dx.doi.org/10.2174/1570164614666170203165022	Print ISSN 1570-1646
Publisher Name Bentham Science Publisher	Online ISSN 1875-6247