Raw data of LlAK enzyme kinetics and molecular interactions between LlAK and EGCG by docking, molecular dynamics and fluorescence quenching
Published: 1 July 2024| Version 1 | DOI: 10.17632/gjtxh3rv9s.1
Contributors:
, , Description
Brown recluse spiders (Loxosceles spp.) can cause serious public health issues. Our study focuses on understanding the enzyme arginine kinase from Loxosceles laeta (LlAK) and exploring the potential of (-)-epigallocatechin gallate (EGCG) as a safer alternative for pest control. In this dataset, we provide raw data and analysis of LlAK enzyme kinetics for arginine and ATP substrates. Additionally, we include information on fluorescence quenching of LlAK and EGCG interaction, LlAK molecular model, and molecular docking between LlAK and EGCG at arginine and ATP binding sites. The molecular dynamics trajectories for the LlAK-EGCG interactions are available from the corresponding authors upon request.
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Institutions
Centro de Investigacion en Alimentacion y Desarrollo AC
Categories
Enzyme Kinetics, Molecular Dynamics, Quenching, Protein Biochemistry, Molecular Interaction, Molecular Docking