Structural and functional characterization of the glutathione peroxidase-like thioredoxin peroxidase from the fungus Trichoderma reesei

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dc.contributorLab. Biofísicapt_BR
dc.contributor.authorAdriani, Patricia P.pt_BR
dc.contributor.authorPaiva, Fernanda C. R. dept_BR
dc.contributor.authorOliveira, Gabriel S. dept_BR
dc.contributor.authorAmanda C. Leitept_BR
dc.contributor.authorSanches, Adriana S.pt_BR
dc.contributor.authorLopes, Adriana Riospt_BR
dc.contributor.authorDias, Marcio V. B.pt_BR
dc.contributor.authorChambergo, Felipe S.pt_BR
dc.date.accessioned2021-02-03T12:47:30Z-
dc.date.available2021-02-03T12:47:30Z-
dc.date.issued2021pt_BR
dc.identifier.citationAdriani PP., Paiva FC.R., Oliveira GS., AC.L, Sanches AS., Lopes AR, et al. Structural and functional characterization of the glutathione peroxidase-like thioredoxin peroxidase from the fungus Trichoderma reesei. Int J Biol Macromol. 2021 Jan;167: 93-100. doi:10.1016/j.ijbiomac.2020.11.179.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/3507-
dc.description.abstractGlutathione peroxidases (GPx) are a family of enzymes with the ability to reduce organic and inorganic hydroperoxides to the corresponding alcohols using glutathione or thioredoxin as an electron donor. Here, we report the functional and structural characterization of a GPx identified in Trichoderma reesei (TrGPx). TrGPx was recombinantly expressed in a bacterial host and purified using affinity. Using a thioredoxin coupled assay, TrGPx exhibited activity of 28 U and 12.5 U in the presence of the substrates H2O2 and t-BOOH, respectively, and no activity was observed when glutathione was used. These results indicated that TrGPx is a thioredoxin peroxidase and hydrolyses H2O2 better than t-BOOH. TrGPx kinetic parameters using a pyrogallol assay resulted at Kmapp = 11.7 mM, Vmaxapp = 10.9 IU/μg TrGPx, kcat = 19 s−1 and a catalytic efficiency of 1.6 mM−1 s−1 to H2O2 as substrate. Besides that, TrGPx demonstrated an optimum pH ranging from 9.0–12.0 and a half-life of 36 min at 80 °C. TrGPx 3D-structure was obtained in a reduced state and non-catalytic conformation. The overall fold is similar to the other phospholipid-hydroperoxide glutathione peroxidases. These data contribute to understand the antioxidant mechanism in fungi and provide information for using antioxidant enzymes in biotechnological applications.pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.format.extent93-100pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofInternational Journal of Biological Macromoleculespt_BR
dc.rightsOpen Accesspt_BR
dc.titleStructural and functional characterization of the glutathione peroxidase-like thioredoxin peroxidase from the fungus Trichoderma reeseipt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.ijbiomac.2020.11.179pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.ijbiomac.2020.11.179pt_BR
dc.contributor.externalUniversidade de São Paulo (USP)pt_BR
dc.contributor.externalUniversity of Warwickpt_BR
dc.identifier.citationvolume167pt_BR
dc.subject.keywordAntioxidantpt_BR
dc.subject.keywordGlutathione peroxidasept_BR
dc.subject.keywordThioredoxinpt_BR
dc.subject.keywordTrichoderma reeseipt_BR
dc.relation.ispartofabbreviatedInt J Biol Macromolpt_BR
dc.identifier.citationabntv. 167, p. 93-100, jan. 2021pt_BR
dc.identifier.citationvancouver2021 Jan;167: 93-100pt_BR
dc.contributor.butantanLopes, Adriana Rios|:Pesquisador:Docente Permanente PPGTOX|:Lab. Biofísicapt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2017/25705-8pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2014/24107-1pt_BR
dc.sponsorship.butantanFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)¦¦2019/05227-0pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦142311/2016-2pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦141090/2016-2pt_BR
dc.sponsorship.butantanConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)¦¦302848/2017-7pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.openairetypeArticle-
item.fulltextCom Texto completo-
item.grantfulltextembargo_29990101-
item.languageiso639-1English-
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