Browsing by Author "Ntie-Kang, Fidele"

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    A computer-based approach for developing linamarase inhibitory agents
    (Walter de Gruyter GmbH, 2020-04-18) Paul, Lucas; Mudogo, Celestin; Mtei, Kelvin; Machunda, Revocatus; Ntie-Kang, Fidele
    Cassava is a strategic crop, especially for developing countries. However, the presence of cyanogenic compounds in cassava products limits the proper nutrients utilization. Due to the poor availability of structure discovery and elucidation in the Protein Data Bank is limiting the full understanding of the enzyme, how to inhibit it and applications in different fields. There is a need to solve the three-dimensional structure (3-D) of linamarase from cassava. The structural elucidation will allow the development of a competitive inhibitor and various industrial applications of the enzyme. The goal of this review is to summarize and present the available 3-D modeling structure of linamarase enzyme using different computational strategies. This approach could help in determining the structure of linamarase and later guide the structure elucidation in silico and experimentally
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    Structural characterization of cassava linamarase-linamarin enzyme complex: an integrated computational approach
    (Journal of Biomolecular Structure and Dynamics, SDG 2: Zero Hunger, SDG 3: Good Health and Well-being, SDG 9: Industry, Innovation, and Infrastructure.) Lucas, Paul; Shadrack, DM; Mudogo, CN; Mtei, KM; Machunda, RL; Ntie-Kang, Fidele
    Cassava linamarase is a hydrolyzing enzyme that belongs to a glycoside hydrolase family 1 (GH1). It is responsible for breaking down linamarin to toxic cyanide. The enzyme provides a defensive mechanism for plants against herbivores and has various applications in many fields. Understanding the structure of linamarase at the molecular level is a key to avail its reaction mechanism. In this study, the three-dimensional (3D) structure of linamarase was built for the first time using homology modelling and used to study its interaction with linamarin. Molecular docking calculations established the binding and orientation nature of linamarin, while molecular dynamics (MD) simulation established protein-ligand complexes' stability. Binding-free energy based on MM/PBSA was further used to rescore the docking results. An ensemble structure was found to be relatively stable compared to the modelled structure. This study sheds light on the exploration of linamarase towards understanding its reaction mechanisms.