Transient binding sites at the surface of haloalkane dehalogenase LinB as locations for fine-tuning enzymatic activity.

ABSTRACT: The haloalkane dehalogenase LinB is a well-known enzyme that contains buried active site and is used for many modelling studies. Using classical molecular dynamics simulations of enzymes and substrates, we searched for transient binding sites on the surface of the LinB protein by calculating maps of enzyme-ligand interactions that were then transformed into sparse matrices. All residues considered as functionally important for enzyme performance (e.g., tunnel entrances) were excluded from the analysis to concentrate rather on non-obvious surface residues. From a set of 130 surface residues, twenty-six were proposed as a promising improvement of enzyme performance. Eventually, based on rational selection and filtering out the potentially unstable mutants, a small library of ten mutants was

SUBMITTER: Raczynska A 

PROVIDER: S-EPMC9956002 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature