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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/59028
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dc.creatorMozart Silvio Pereirapt_BR
dc.creatorSimara Semíramis de Araújopt_BR
dc.creatorRonaldo Alves Pinto Nagempt_BR
dc.creatorJohn P. Richardpt_BR
dc.creatorTiago Antônio da Silva Brandãopt_BR
dc.date.accessioned2023-09-29T12:14:58Z-
dc.date.available2023-09-29T12:14:58Z-
dc.date.issued2022-
dc.citation.volume119pt_BR
dc.identifier.doihttps://doi.org/10.1016/j.bioorg.2021.105561pt_BR
dc.identifier.issn1090-2120pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/59028-
dc.description.resumoSalicylate hydroxylase (NahG) has a single redox site in which FAD is reduced by NADH, the O2 is activated by the reduced flavin, and salicylate undergoes an oxidative decarboxylation by a C(4a)-hydroperoxyflavin intermediate to give catechol. We report experimental results that show the contribution of individual pieces of the FAD cofactor to the observed enzymatic activity for turnover of the whole cofactor. A comparison of the kinetic parameters and products for the NahG-catalyzed reactions of FMN and riboflavin cofactor fragments reveal that the adenosine monophosphate (AMP) and ribitol phosphate pieces of FAD act to anchor the flavin to the enzyme and to direct the partitioning of the C(4a)-hydroperoxyflavin reaction intermediate towards hydroxylation of salicylate. The addition of AMP or ribitol phosphate pieces to solutions of the truncated flavins results in a partial restoration of the enzymatic activity lost upon truncation of FAD, and the pieces direct the reaction of the C(4a)-hydroperoxyflavin intermediate towards hydroxylation of salicylate.pt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_BR
dc.description.sponsorshipINCT – Instituto nacional de ciência e tecnologia (Antigo Instituto do Milênio)pt_BR
dc.description.sponsorshipOutra Agênciapt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICB - DEPARTAMENTO DE BIOQUÍMICA E IMUNOLOGIApt_BR
dc.publisher.departmentICX - DEPARTAMENTO DE QUÍMICApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofBioorganic Chemistrypt_BR
dc.rightsAcesso Restritopt_BR
dc.subjectOne-component flavoprotein monooxygenasept_BR
dc.subjectFlavoenzymept_BR
dc.subjectActivationpt_BR
dc.subjectOxidoreductasespt_BR
dc.subjectBiocatalysispt_BR
dc.subject.otherAnálise enzimáticapt_BR
dc.subject.otherEnzimas - Regulaçãopt_BR
dc.subject.otherCinética de enzimaspt_BR
dc.subject.otherMecanismos de reações orgânicaspt_BR
dc.subject.otherReações químicaspt_BR
dc.subject.otherBioquímicapt_BR
dc.titleThe role of remote flavin adenine dinucleotide pieces in the oxidative decarboxylation catalyzed by salicylate hydroxylasept_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S0045206821009391pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-1550-8013pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-7219-1625pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-0440-2387pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-7783-3014pt_BR
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