| _version_ | 1866901681224024064 |
|---|---|
| author | Dr. T. Sharmila Raj Nandhini R Calista Stephanie A Vyshali S Anugraha J |
| author_facet | Dr. T. Sharmila Raj Nandhini R Calista Stephanie A Vyshali S Anugraha J |
| contents | <p>Bifunctional enzymes catalyze two distinct biochemical reactions in one protein and are therefore effective regulators of cellular functions. Here, describes an integrated computational workflow for the analysis of these enzymes. Firstly, downloading protein sequences from the NCBI database. To learn about their dual activity, we identified the respective protein domains that cause each catalytic function through InterProScan. Then modeled three-dimensional structures of the enzymes through SWISS-MODEL. Active site analysis was done using CASTp to identify where substrates bind. Molecular docking simulations through ClusPro were employed to visualize substrate interactions with each active site. The stability of these complexes and the dynamics of the whole protein were evaluated by molecular dynamics simulations with GROMACS. Lastly, in order to examine their evolutionary past, we built phylogenetic trees with MEGA and PhyML. Multidisciplinary approach presents a detailed roadmap for clarifying how structure informs bifunctionality, providing important information for drug discovery and metabolic engineering.</p> |
| format | Recurso digital |
| id | zenodo_https___doi_org_10_5281_zenodo_18007104 |
| institution | Zenodo |
| language | |
| publishDate | 2025 |
| publisher | Zenodo |
| record_format | zenodo |
| spellingShingle | AN INTEGRATED COMPUTATIONAL ANALYSIS OF BIFUNCTIONAL ENZYMES (CELLULASE-XYLANASE) Dr. T. Sharmila Raj Nandhini R Calista Stephanie A Vyshali S Anugraha J <p>Bifunctional enzymes catalyze two distinct biochemical reactions in one protein and are therefore effective regulators of cellular functions. Here, describes an integrated computational workflow for the analysis of these enzymes. Firstly, downloading protein sequences from the NCBI database. To learn about their dual activity, we identified the respective protein domains that cause each catalytic function through InterProScan. Then modeled three-dimensional structures of the enzymes through SWISS-MODEL. Active site analysis was done using CASTp to identify where substrates bind. Molecular docking simulations through ClusPro were employed to visualize substrate interactions with each active site. The stability of these complexes and the dynamics of the whole protein were evaluated by molecular dynamics simulations with GROMACS. Lastly, in order to examine their evolutionary past, we built phylogenetic trees with MEGA and PhyML. Multidisciplinary approach presents a detailed roadmap for clarifying how structure informs bifunctionality, providing important information for drug discovery and metabolic engineering.</p> |
| title | AN INTEGRATED COMPUTATIONAL ANALYSIS OF BIFUNCTIONAL ENZYMES (CELLULASE-XYLANASE) |
| url | https://doi.org/10.5281/zenodo.18007104 |