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dc.contributor.authorIzidoro, M.A.
dc.contributor.authorAssis, D.M.
dc.contributor.authorLindberg, I.
dc.date.accessioned2020-03-27T15:13:19Z
dc.date.available2020-03-27T15:13:19Z
dc.date.issued2010
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-77957605073&doi=10.1515%2fBC.2010.114&partnerID=40&md5=2db9b684a71c6ee16b981eb6d1f82490
dc.identifier.urihttp://hdl.handle.net/10713/12431
dc.description.abstractHere we report a detailed analysis of magnesium (Mg2+) ion effects on furin hydrolysis of fluorescent resonance energy transfer decapeptide substrates derived from canonical R-X-K/R-R furin cleavage motifs within certain viral envelope glycoproteins and eukaryotic proproteins. Using virus-derived sequences a selective activation of furin by Mg2+ ions was observed as a result of cooperativity between furin subsites. Furin hydrolysis of the peptides Abz-SRRHKR?FAGV-Q-EDDnp (from measles virus fusion protein Fo) and Abz-RERRRKKR?GLFG-Q-EDDnp (from Asian avian influenza A, H5N1) was activated between 60-and 80-fold by MgCl 2. It appears that virus envelope glycoprotein mutations have been selected to increase their susceptibility to furin within cells, a location where Mg2+ is present in adequate concentrations for activation. Both the pH profile of furin and its intrinsic fluorescence were modified by Mg 2+ ions, which bind to furin with a Kd value of 1.1 mm.en_US
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico, CNPq, Fundação de Amparo à Pesquisa do Estado de São Paulo, FAPESPen_US
dc.description.urihttps://doi.org/10.1515/BC.2010.114en_US
dc.language.isoen_USen_US
dc.relation.ispartofBiological Chemistry
dc.subjectfluorescenceen_US
dc.subjectmagnesiumen_US
dc.subjectpeptidaseen_US
dc.subjectproteaseen_US
dc.titleEffects of magnesium ions on recombinant human furin: Selective activation of hydrolytic activity upon substrates derived from virus envelope glycoproteinen_US
dc.typeArticleen_US
dc.identifier.doi10.1515/BC.2010.114
dc.identifier.pmid20635860
dc.identifier.ispublishedYes
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