Research Article
Investigation of Halide Ion Release Tunnels of Haloalcohol Dehalogenase from Agrobacterium Radiobacter AD1; Computational Study
@INPROCEEDINGS{10.1007/978-3-030-93712-6_25, author={Aweke Mulu Belachew and Tang Laxia}, title={Investigation of Halide Ion Release Tunnels of Haloalcohol Dehalogenase from Agrobacterium Radiobacter AD1; Computational Study}, proceedings={Advances of Science and Technology. 9th EAI International Conference, ICAST 2021, Hybrid Event, Bahir Dar, Ethiopia, August 27--29, 2021, Proceedings, Part II}, proceedings_a={ICAST PART 2}, year={2022}, month={1}, keywords={Halide ion release tunnels Halohydrine dehalogenase Caver Molecular dynamic simulation}, doi={10.1007/978-3-030-93712-6_25} }- Aweke Mulu Belachew
Tang Laxia
Year: 2022
Investigation of Halide Ion Release Tunnels of Haloalcohol Dehalogenase from Agrobacterium Radiobacter AD1; Computational Study
ICAST PART 2
Springer
DOI: 10.1007/978-3-030-93712-6_25
Abstract
The Halohydrine dehalogenase (HheC), active site is buried deep inside the structure of the enzyme and to enter the active site, the substrate must cross via the body of the enzyme called tunnels. In several studies revealed that they have been influenced substrate selectivity, stability and activity of enzymes. Know a day, identifying and understanding how tunnels exert selectivity, stability, and activity regulation of enzymes have been growing interest in the fields of computational approach and enzyme engineering. As far as, the HheC concerned studies suggest that the release of chloride ion determines the overall activity of the enzyme and thus tunnels are assumed to exist. Swiss-Modell, Auto dock 3.2, Gromacs 5.2.1, Caver 3.0, and RAMD computational techniques were applied to identify and analyze tunnels and how chloride ions migrate through these tunnels. The purpose of this study is to identify tunnels and analyzes how to influence Chloride ion-releasing activity in the HheC enzyme and provide prerequisite data for wet-lab experiment used to improve overall activity. In this study, we found the presence of Chloride ion narrowed tunnels compare to free HheC enzyme. Moreover, conformation difference, tunnel lining residues and bottle-neck residues were identified for next wet-lab experiment. Future wet-lab investigations to validate the role of residues that are found in tunnel lining could be needed to engineer the activity of HheC.
