Show simple item record

dc.contributor.authorPaul, Lucas
dc.contributor.authorShadrack, Daniel
dc.contributor.authorMudogo, Celestin
dc.contributor.authorMtei, Kelvin
dc.contributor.authorMachunda, Revocatus
dc.contributor.authorNtie‐Kang, Fidele
dc.date.accessioned2022-09-22T11:12:40Z
dc.date.available2022-09-22T11:12:40Z
dc.date.issued2021-05-21
dc.identifier.urihttps://doi.org/10.1080/07391102.2021.1925156
dc.identifier.urihttps://dspace.nm-aist.ac.tz/handle/20.500.12479/1675
dc.descriptionThis research article was published by Taylor & Francis Group., 2021en_US
dc.description.abstractCassava 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. Communicated by Ramaswamy H. Sarmaen_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Groupen_US
dc.subjectLinamaraseen_US
dc.subjectLinamarinen_US
dc.subjectMolecular dynamics simulationen_US
dc.subjectMolecular dockingen_US
dc.subjectCassavaen_US
dc.titleStructural characterization of cassava linamarase-linamarin enzyme complex: an integrated computational approachen_US
dc.typeArticleen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record