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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/59026
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dc.creatorJudith R. Cristobalpt_BR
dc.creatorTiago Antônio da Silva Brandãopt_BR
dc.creatorArchie C. Reyespt_BR
dc.creatorJohn P. Richardpt_BR
dc.date.accessioned2023-09-29T12:08:00Z-
dc.date.available2023-09-29T12:08:00Z-
dc.date.issued2021-
dc.citation.volume60pt_BR
dc.citation.issue45pt_BR
dc.citation.spage3362pt_BR
dc.citation.epage3373pt_BR
dc.identifier.doihttps://doi.org/10.1021/acs.biochem.1c00589pt_BR
dc.identifier.issn1520-4995pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/59026-
dc.description.resumoThe role of a global, substrate-driven, enzyme conformational change in enabling the extraordinarily large rate acceleration for orotidine 5′-monophosphate decarboxylase (OMPDC)-catalyzed decarboxylation of orotidine 5′-monophosphate(OMP) is examined in experiments that focus on the interactions between OMPDC and the ribosyl hydroxyl groups ofOMP. TheD37 and T100′side chains of OMPDC interact, respectively, with the C-3′and C-2′hydroxyl groups of enzyme-boundOMP.D37G and T100′A substitutions result in 1.4 kcal/mol increases in the activation barrier ΔG⧧for catalysis of decarboxylation of thephosphodianion-truncated substrate 1-(β-D-erythrofuranosyl) orotic acid (EO) but result in larger 2.1−2.9 kcal/mol increases in ΔG⧧for decarboxylation of OMPand for phosphite dianion-activated decarboxylation of EO. This shows that these substitutions reduce transition-state stabilization by the Q215, Y217, and R235 side chains at the dianion binding site. The D37G and T100′A substitutions result in <1.0 kcal/mol increases in ΔG⧧ for activation of OMPDC-catalyzed decarboxylation of the phosphoribofuranosyl-truncated substrate FO by phosphite dianions. Experiments to probe the effect of D37 and T100′substitutions on the kinetic parameters for D-glycerol 3-phosphate and D-erythritol 4-phosphate activators of OMPDC-catalyzed decarboxylation of FO show that ΔG⧧for sugar phosphate-activated reactions is increased byca.2.5 kcal/mol for each −OH interaction eliminated by D37G or T100′A substitutions. We conclude that the interactions between the D37 and T100′side chainsand ribosyl or ribosyl-like hydroxyl groups are utilized to activate OMPDC for catalysis of decarboxylation of OMP, EO, and FO.pt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICX - DEPARTAMENTO DE QUÍMICApt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofBiochemistrypt_BR
dc.rightsAcesso Restritopt_BR
dc.subjectChemical reactionspt_BR
dc.subjectKinetic parameterspt_BR
dc.subjectOrganic reactionspt_BR
dc.subjectPeptides and proteinspt_BR
dc.subjectStabilizationpt_BR
dc.subject.otherProteinaspt_BR
dc.subject.otherAnálise enzimáticapt_BR
dc.subject.otherCinética de enzimaspt_BR
dc.subject.otherMecanismos de reações orgânicaspt_BR
dc.subject.otherReações químicaspt_BR
dc.subject.otherBioquímicapt_BR
dc.titleProtein-ribofuranosyl interactions activate orotidine 5′-monophosphate decarboxylase for catalysispt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://pubs.acs.org/doi/10.1021/acs.biochem.1c00589pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-7783-3014pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-9955-393Xpt_BR
dc.identifier.orcidhttps://orcid.org/0000-0002-0440-2387pt_BR
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