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All Journal Journal of Tropical Life Science : International Journal of Theoretical, Experimental, and Applied Life Sciences
Oladipo, Oluwatosin
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Agriculture, Biological Sciences & Forestry Environmental Science

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Structural Comparison of α-agarase (α-AgaD) from Thalassomonas sp. LD5: An in-silico study: Structural Comparison of α-agarase (α-AgaD) from Thalassomonas sp. LD5 Oyewusi, Habeebat Adekilekun; Oladipo, Oluwatosin; Abdul Wahab, Roswanira; Adekilekun , Habeebulahi Ajibola; Wayan Gunam, Ida Bagus; Huyop, Fahrul
Journal of Tropical Life Science Vol. 15 No. 2
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/

Abstract

The significance of agarase enzymes spans various high-value industries, including food, cosmetics, and medicine. These enzymes play a crucial role in the hydrolysis of agar to produce bioactive oligosaccharides, enabling wide-ranging applications across multiple fields. Among them, α-AgaD is a novel α-agarase enzyme produced by the Thalassomonas sp. LD5 strain. However, the structural and functional characteristics of α-AgaD within biological systems remain largely unexplored. This study therefore aims to provide a comprehensive in silico analysis of α-AgaD, focusing on its physicochemical properties, phylogenetic relationships, secondary structure composition, and 3D homology modelling. A range of computational tools was employed to validate the findings and enhance the structural understanding of this newly identified α-AgaD enzyme. The α-AgaD protein consists of 1,466 amino acids with a molecular weight of 158,787.82 Da. It has a theoretical isoelectric point (pI) of 4.14, indicating an overall acidic nature. Structural analysis revealed that alpha helices and random coils are the predominant secondary structures. Hydrophobic amino acids were more abundant than hydrophilic ones, with glycine accounting for approximately 10.4% of the total residues. The protein's aliphatic index was 72.05, and the instability index was 28.28, suggesting that α-AgaD is stable and likely to maintain its structure across a wide temperature range. Three-dimensional models of α-AgaD were constructed using I-TASSER, NCBI-PDB, SWISS-MODEL, and AlphaFold2, and subsequently validated using ERRAT, Verify3D, and PROCHECK. Among the models generated, AlphaFold2 produced the most accurate prediction, with nearly all amino acid residues located in the preferred regions of the Ramachandran plot. This further confirmed the reliability and quality of the refined models. The in silico structural analysis of α-AgaD offers valuable insights into the enzyme’s primary sequence, functional domains, and overall structural architecture, enhancing our understanding of α-agarase from Thalassomonas sp. LD5.
Concerted Structural analysis predictions of an organohalide pollutants uptake enzyme, putative permease protein (DehHsAADcPt) from Halomonas smyrnensis AAD6T.: Comparative Structural Prediction of putative permease protein (DehHsAADcPt) Oyewusi, Habeebat Adekilekun; Oladipo, Oluwatosin; Adekilekun, Habeebulahi; Abdul Wahab, Roswanira; Akinyede, Kolajo; Oladimeji Tugbobo, Samuel; Wayan Gunam, Ida Bagus; Huyop, Fahrul
Journal of Tropical Life Science Vol. 15 No. 3
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.15.03.07

Abstract

Halomonas smyrnensis AAD6T is a halophilic bacterium capable of utilizing haloalkanoic acid and possessing a specific gene for the uptake of organohalide pollutants. This distinctive characteristic has garnered the attention of researchers who seek to understand the underlying mechanisms. Among its genome, a putative permease protein known as DehHsAADcPt has been identified as a potential candidate for facilitating the uptake of these pollutants. Structural predictions of DehHsAADcPt have been conducted to gain a better understanding of its potential role in pollutant uptake. The predictions of DehHsAADcPt's structural characteristics, presented in this study, shed light on its potential application in bioremediation efforts. The implications of these findings are discussed in detail. The in-silico characterization and functional analysis of DehHsAADcPt was carried out with different bio-computational tools or servers. DehHsAADcPt belongs to the ABC inner membrane transporter permease family protein that is highly basic, hydrophobic, and thermostable having a molecular weight of 58,885.47Da as revealed from ExPASy server. The DehHsAADcPt compost mostly alpha helix structure and functional motif belongs to the binding-protein-dependent transport system inner membrane components and phage shock protein family. The 3-D structure obtained by AlphaFold2 homology modeling program and verified by Ramachandran plot revealed that most of the residues are in the allowed or favored regions of the plot. Likewise, several amino acid residues are predicted as ligand binding residues and most of them are highly conserved. The different computational tools used have proven to give holistic structural analysis predictions of DehHsAADcPt and revealed the concerted nature of these tools in elucidation. This study provides valuable insights into the structural and functional properties of DehHsAADcPt protein, which could pave the way for its potential application in the bioremediation of halogenated organic pollutants.
Co-Authors Abdul Wahab, Roswanira Adekilekun , Habeebulahi Ajibola Adekilekun, Habeebulahi Akinyede, Kolajo Huyop, Fahrul Ida Bagus Wayan Gunam Oladimeji Tugbobo, Samuel Oyewusi, Habeebat Adekilekun