A novel mechanism of β-glucosidase stimulation through a monosaccharide binding-induced conformational change

Página do item simplificado
dc.creatorThamy Lívia Ribeiro Corrêa
dc.creatorJoão Paulo Lourenço Franco Cairo
dc.creatorJúnio Cota Silva
dc.creatorAndré Ricardo de Lima Damasio
dc.creatorLeandro Cristante de Oliveira
dc.creatorFabio Marcio Squina
dc.date.accessioned2023-04-27T16:20:51Z
dc.date.accessioned2025-09-08T23:34:04Z
dc.date.available2023-04-27T16:20:51Z
dc.date.issued2021
dc.identifier.doihttps://doi.org/10.1016/j.ijbiomac.2020.11.001
dc.identifier.issn0141-8130
dc.identifier.urihttps://hdl.handle.net/1843/52587
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofInternational Journal of Biological Macromolecules
dc.rightsAcesso Restrito
dc.subjectMonossacarideos
dc.subjectCombustiveis fosseis
dc.subjectEnzimas
dc.subject.otherBioeconomy
dc.subject.otherβ-Glucosidases
dc.subject.otherGH1
dc.subject.otherThermotoga petrophila
dc.subject.otherMolecular dynamics simulation
dc.titleA novel mechanism of β-glucosidase stimulation through a monosaccharide binding-induced conformational change
dc.typeArtigo de periódico
local.citation.epage1196
local.citation.spage1188
local.citation.volume166
local.description.resumoIt is urgent the transition from a fossil fuel-based economy to a sustainable bioeconomy based on bioconversion technologies using renewable plant biomass feedstocks to produce high chemicals, bioplastics, and biofuels. β- Glucosidases are key enzymes responsible for degrading the plant cell wall polymers, as they cleave glucan- based oligo- and polysaccharides to generate glucose. Monosaccharide-tolerant or -stimulated β-glucosidases have been reported in the past decade. Here, we describe a novel mechanism of β-glucosidase stimulation by glucose and xylose. The glycoside hydrolase 1 family β-glucosidase from Thermotoga petrophila (TpBgl1) displays a typical glucose stimulation mechanism based on an increased Vmax and decreased Km in response to glucose. Through molecular docking and dynamics analyses, we mapped putative monosaccharide binding regions (BRs) on the surface of TpBgl1. Our results indicate that after interaction with glucose or xylose at BR1 site, an adjacent loop region assumes an extended conformation, which increases the entrance to the TpBgl1 active site, improving product formation. Biochemical assays with TpBgl1 BR1 mutants, TpBgl1D49A/Y410A and TpBgl1- D49K/Y410H, resulted in decreasing and abolishing monosaccharide stimulation, respectively. These mutations also impaired the BR1 looping extension responsible for monosaccharide stimulation. This study provides a molecular basis for the rational design of β-glucosidases for biotechnological applications.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0141813020349266

Arquivos

Licença do pacote

Agora exibindo 1 - 1 de 1
Imagem de Miniatura
Nome:
License.txt
Tamanho:
1.99 KB
Formato:
Plain Text
Descrição:
Baixar

Coleções

Artigo de Periódico

Logo UFMG