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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleP-i Class Metalloproteinase From Bothrops Moojeni Venom Is A Post-proline Cleaving Peptidase With Kininogenase Activity: Insights Into Substrate Selectivity And Kinetic Behaviorpt_BR
dc.contributor.authorOkamoto D.N.pt_BR
dc.contributor.authorKondo M.Y.pt_BR
dc.contributor.authorOliveira L.C.G.pt_BR
dc.contributor.authorHonorato R.V.pt_BR
dc.contributor.authorZanphorlin L.M.pt_BR
dc.contributor.authorCoronado M.A.pt_BR
dc.contributor.authorAraujo M.S.pt_BR
dc.contributor.authorDa Motta G.pt_BR
dc.contributor.authorVeronez C.L.pt_BR
dc.contributor.authorAndrade S.S.pt_BR
dc.contributor.authorOliveira P.S.L.pt_BR
dc.contributor.authorArni R.K.pt_BR
dc.contributor.authorCintra A.C.O.pt_BR
dc.contributor.authorSampaio S.V.pt_BR
dc.contributor.authorJuliano M.A.pt_BR
dc.contributor.authorJuliano L.pt_BR
dc.contributor.authorMurakami M.T.pt_BR
dc.contributor.authorGouvea I.E.pt_BR
unicamp.authorZanphorlin, L.M., Departamento de Orgânica, Instituto de Química, UNICAMP, 13083-970 Campinas, Brazilpt_BR
unicamp.author.externalOkamoto, D.N., Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalKondo, M.Y., Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalOliveira, L.C.G., Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalHonorato, R.V., Laboratório Nacional de Biociências, CNPEM, Rua Giuseppe Maximo Scolfaro, 10000, Campinas 13083-970, Brazilpt
unicamp.author.externalCoronado, M.A., Departamento de Física, IBILCE, UNESP, 15054-000 São José do Rio Preto, Brazilpt
unicamp.author.externalAraújo, M.S., Departamento de Bioquímica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalDa Motta, G., Departamento de Bioquímica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalVeronez, C.L., Departamento de Bioquímica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalAndrade, S.S., Departamento de Ginecologia, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalOliveira, P.S.L., Laboratório Nacional de Biociências, CNPEM, Rua Giuseppe Maximo Scolfaro, 10000, Campinas 13083-970, Brazilpt
unicamp.author.externalArni, R.K., Departamento de Física, IBILCE, UNESP, 15054-000 São José do Rio Preto, Brazilpt
unicamp.author.externalCintra, A.C.O., Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto-USP, 14040-903 Ribeirão Preto, SP, Brazilpt
unicamp.author.externalSampaio, S.V., Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto-USP, 14040-903 Ribeirão Preto, SP, Brazilpt
unicamp.author.externalJuliano, M.A., Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalJuliano, L., Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
unicamp.author.externalMurakami, M.T., Laboratório Nacional de Biociências, CNPEM, Rua Giuseppe Maximo Scolfaro, 10000, Campinas 13083-970, Brazilpt
unicamp.author.externalGouvea, I.E., Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazilpt
dc.description.abstractSnake venom metalloproteinases (SVMPs) belonging to P-I class are able to hydrolyze extracellular matrix proteins and coagulation factors triggering local and systemic reactions by multiple molecular mechanisms that are not fully understood. BmooMPα-I, a P-I class SMVP from Bothrops moojeni venom, was active upon neuro- and vaso-active peptides including angiotensin I, bradykinin, neurotensin, oxytocin and substance P. Interestingly, BmooMPα-I showed a strong bias towards hydrolysis after proline residues, which is unusual for most of characterized peptidases. Moreover, the enzyme showed kininogenase activity similar to that observed in plasma and cells by kallikrein. FRET peptide assays indicated a relative promiscuity at its S2-S′2 subsites, with proline determining the scissile bond. This unusual post-proline cleaving activity was confirmed by the efficient hydrolysis of the synthetic combinatorial library MCA-GXXPXXQ-EDDnp, described as resistant for canonical peptidases, only after Pro residues. Structural analysis of the tripeptide LPL complexed with BmooMPα-I, generated by molecular dynamics simulations, assisted in defining the subsites and provided the structural basis for subsite preferences such as the restriction of basic residues at the S2 subsite due to repulsive electrostatic effects and the steric impediment for large aliphatic or aromatic side chains at the S1 subsite. These new functional and structural findings provided a further understanding of the molecular mechanisms governing the physiological effects of this important class of enzymes in envenomation process. © 2014 Elsevier B.V.en
dc.relation.ispartofBiochimica et Biophysica Acta - Proteins and Proteomicspt_BR
dc.date.issued2014pt_BR
dc.identifier.citationBiochimica Et Biophysica Acta - Proteins And Proteomics. , v. 1844, n. 3, p. 545 - 552, 2014.pt_BR
dc.language.isoenpt_BR
dc.description.volume1844pt_BR
dc.description.issuenumber3pt_BR
dc.description.firstpage545pt_BR
dc.description.lastpage552pt_BR
dc.rightsfechadopt_BR
dc.sourceScopuspt_BR
dc.identifier.issn15709639pt_BR
dc.identifier.doi10.1016/j.bbapap.2013.12.014pt_BR
dc.identifier.urlhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84892940190&partnerID=40&md5=986c570d6686ca3b321a1cf5befa316fpt_BR
dc.date.available2015-06-25T17:53:29Z
dc.date.available2015-11-26T14:25:12Z-
dc.date.accessioned2015-06-25T17:53:29Z
dc.date.accessioned2015-11-26T14:25:12Z-
dc.description.provenanceMade available in DSpace on 2015-06-25T17:53:29Z (GMT). No. of bitstreams: 0 Previous issue date: 2014en
dc.description.provenanceMade available in DSpace on 2015-11-26T14:25:12Z (GMT). No. of bitstreams: 0 Previous issue date: 2014en
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/86465
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/86465-
dc.identifier.idScopus2-s2.0-84892940190pt_BR
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