Engineering Highly Active D-Pantothenate Esterase: A Silicon-Based Approach and Molecular Insights

Engineering Highly Active D-Pantothenate Esterase: A Silicon-Based Approach and Molecular Insights

This study presents a novel approach to enhance the activity of D-pantothenate esterase using silicon-based engineering. D-pantothenate esterase plays a crucial role in the biosynthesis of pantothenic acid (vitamin B5), an essential nutrient for various metabolic processes. Enhancing its activity holds significant potential for industrial applications, particularly in the pharmaceutical and food industries.

Here, we employed a combination of computational and experimental methods to engineer D-pantothenate esterase with improved activity. We first utilized molecular docking and molecular dynamics simulations to screen a library of silicon-containing compounds for their potential to interact with and stabilize the enzyme's active site. Promising candidates identified through these in silico studies were then tested experimentally.

Our results demonstrate successful enhancement of D-pantothenate esterase activity upon introducing specific silicon-based modifications. We further investigated the molecular basis of this enhanced activity using various spectroscopic techniques and computational analyses. These analyses revealed key interactions between the introduced silicon moieties and the enzyme's active site residues, providing valuable insights into the mechanism of activity enhancement.

The findings of this study provide a novel strategy for engineering D-pantothenate esterase with enhanced activity. The insights gained from understanding the molecular basis of this enhancement pave the way for further development of highly efficient biocatalysts for industrial applications.