Glycosylation and charge distribution orchestrates the conformational ensembles of a biotechnologically promissory phytase in different pHs: a computational study

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dc.creatorThaís Paiva Porto de Souza
dc.creatorLetícia Xavier Silva Cantão
dc.creatorMarina Quádrio Raposo Branco Rodrigues
dc.creatorDaniel Bonoto Gonçalves
dc.creatorRonaldo Alves Pinto Nagem
dc.creatorRafael Eduardo Oliveira Rocha
dc.creatorRenato Ramos Godoi
dc.creatorWilliam James Nogueira Lima
dc.creatorAlexsandro Sobreira Galdino
dc.creatorRaquel Cardoso de Melo Minardi
dc.creatorLeonardo Henrique França de Lima
dc.date.accessioned2024-10-14T23:23:13Z
dc.date.accessioned2025-09-09T00:53:28Z
dc.date.available2024-10-14T23:23:13Z
dc.date.issued2023-06-16
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.identifier.doihttps://doi.org/10.1080/07391102.2023.2223685
dc.identifier.issn1538-0254
dc.identifier.urihttps://hdl.handle.net/1843/77437
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofJournal of Biomolecular Structure and Dynamics
dc.rightsAcesso Restrito
dc.subjectBiotecnologia
dc.subjectFosfatases
dc.subjectAspergillus nidulans
dc.subjectProdutos finais de glicosilação
dc.titleGlycosylation and charge distribution orchestrates the conformational ensembles of a biotechnologically promissory phytase in different pHs: a computational study
dc.typeArtigo de periódico
local.citation.epage5041
local.citation.issue10
local.citation.spage5030
local.citation.volume42
local.description.resumoPhytases [myo-inositol(1,2,3,4,5,6) hexakisphosphate phosphohydrolases] are phytate-specific phosphatases not present in monogastric animals. Nevertheless, they are an essential supplement to feeding such animals and for human special diets. It is crucial, hence, the biotechnological use of phytases with intrinsic stability and activity at the acid pHs from gastric environments. Here we use Metadynamics (METADY) simulations to probe the conformational space of the Aspergillus nidulans phytase and the differential effects of pH and glycosylation in this same space. The results suggest that strategic combinations of pH and glycosylation affect the stability of native-like conformations and alternate these structures from a metastable to a stable profile. Furthermore, the protein segments previously reported as more thermosensitive in phytases from this family present a pivotal role in the conformational changes at different conditions, especially H2, H5-7, L8, L10, L12, and L17. Also, the glycosylations and the pH-dependent charge balance modulate the mobility and interactions at these same regions, with consequences for the surface solvation and active site exposition. Finally, although the glycosylations have stabilized the native structure and improved the substrate docking at all the studied pHs, the data suggest a higher phytate receptivity at catalytic poses for the unglycosylated structure at pH 6.5 and the glycosylated one at pH 4.5. This behavior agrees with the exact change in optimum pH reported for this enzyme, expressed on low or high glycosylating systems. We hope the results and insights presented here will be helpful in future approaches for rational engineering of technologically promising phytases and intelligent planning of their heterologous expression systems and conditions for use.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.departmentICB - DEPARTAMENTO DE BIOQUÍMICA E IMUNOLOGIA
local.publisher.initialsUFMG
local.url.externahttps://www.tandfonline.com/doi/full/10.1080/07391102.2023.2223685

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