Exploring the Structural Insights of Thermostable Geobacillus esterases by Computational Characterization.

ABSTRACT: This study conducted an in silico analysis of two biochemically characterized thermostable esterases, Est2 and Est3, from Geobacillus strains. To achieve this, the amino acid sequences of Est2 and Est3 were examined to assess their biophysicochemical properties, evolutionary connections, and sequence similarities. Three-dimensional models were constructed and validated through diverse bioinformatics tools. Molecular dynamics (MD) simulation was employed on a pNP-C2 ligand to explore interactions between enzymes and ligand. Biophysicochemical property analysis indicated that aliphatic indices and theoretical T _m values of enzymes were between 82-83 and 55-65 °C, respectively. Molecular phylogeny placed Est2 and Est3 within Family XIII, alongside other

SUBMITTER: Surmeli Y 

PROVIDER: S-EPMC11292637 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature