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Molecular insights of a xyloglucan endo-transglycosylase/hydrolase of radiata pine (PrXTH1) expressed in response to inclination: Kinetics and computational study

dc.contributor.authorMorales-Quintana L.
dc.contributor.authorCarrasco-Orellana C.
dc.contributor.authorBeltrán D.
dc.contributor.authorMoya-León M.A.
dc.contributor.authorHerrera R.
dc.date.accessioned2020-09-02T22:23:39Z
dc.date.available2020-09-02T22:23:39Z
dc.date.issued2019
dc.identifier10.1016/j.plaphy.2019.01.016
dc.identifier.citation136, , 155-161
dc.identifier.issn09819428
dc.identifier.urihttps://hdl.handle.net/20.500.12728/5438
dc.descriptionXyloglucan endotransglycosylase/hydrolases (XTH) may have endotransglycosylase (XET) and/or hydrolase (XEH) activities. Previous studies confirmed XET activity for PrXTH1 protein from radiata pine. XTHs could interact with many hemicellulose substrates, but the favorite substrate of PrXTH1 is still unknown. The prediction of union type and energy stability of the complexes formed between PrXTH1 and different substrates (XXXGXXXG, XXFGXXFG, XLFGXLFG and cellulose) were determined using bioinformatics tools. Molecular Docking, Molecular Dynamics, MM-GBSA and Electrostatic Potential Calculations were employed to predict the binding modes, free energies of interaction and the distribution of electrostatic charge. The results suggest that the enzyme formed more stable complexes with hemicellulose substrates than cellulose, and the best ligand was the xyloglucan XLFGXLFG (free energy of −58.83 ± 0.8 kcal mol−1). During molecular dynamics trajectories, hemicellulose fibers showed greater stability than cellulose. Aditionally, the kinetic properties of PrXTH1 enzyme were determined. The recombinant protein was active and showed an optimal pH 5.0 and optimal temperature of 37 °C. A Km value of 20.9 mM was determined for xyloglucan oligomer. PrXTH1 is able to interact with different xyloglycans structures but no activity was observed for cellulose as substrate, remodeling cell wall structure in response to inclination. © 2019 Elsevier Masson SAS
dc.language.isoen
dc.publisherElsevier Masson SAS
dc.subjectEnzymatic parameters
dc.subjectPlant cell wall
dc.subjectXyloglucan endotransglycosylase/hydrolases
dc.subjectXyloglycans
dc.subjectglycosyltransferase
dc.subjectplant protein
dc.subjectrecombinant protein
dc.subjectxyloglucan endotransglycosylase
dc.subjectcell wall
dc.subjectenzyme specificity
dc.subjectenzymology
dc.subjectgene expression regulation
dc.subjectkinetics
dc.subjectmetabolism
dc.subjectmolecular cloning
dc.subjectmolecular docking
dc.subjectphysiology
dc.subjectPichia
dc.subjectCell Wall
dc.subjectCloning, Molecular
dc.subjectGene Expression Regulation, Plant
dc.subjectGlycosyltransferases
dc.subjectKinetics
dc.subjectMolecular Docking Simulation
dc.subjectPichia
dc.subjectPlant Proteins
dc.subjectRecombinant Proteins
dc.subjectSubstrate Specificity
dc.titleMolecular insights of a xyloglucan endo-transglycosylase/hydrolase of radiata pine (PrXTH1) expressed in response to inclination: Kinetics and computational study
dc.typeArticle


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