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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 Behavior.pt_BR
dc.contributor.authorOkamoto, Débora Npt_BR
dc.contributor.authorKondo, Marcia Ypt_BR
dc.contributor.authorOliveira, Lilian C Gpt_BR
dc.contributor.authorHonorato, Rodrigo Vpt_BR
dc.contributor.authorZanphorlin, Leticia Mpt_BR
dc.contributor.authorCoronado, Monika Apt_BR
dc.contributor.authorAraújo, Mariana Spt_BR
dc.contributor.authorda Motta, Guacyarapt_BR
dc.contributor.authorVeronez, Camila Lpt_BR
dc.contributor.authorAndrade, Sheila Spt_BR
dc.contributor.authorOliveira, Paulo S Lpt_BR
dc.contributor.authorArni, Raghuvir Kpt_BR
dc.contributor.authorCintra, Adelia C Opt_BR
dc.contributor.authorSampaio, Suely Vpt_BR
dc.contributor.authorJuliano, Maria Apt_BR
dc.contributor.authorJuliano, Luizpt_BR
dc.contributor.authorMurakami, Mário Tpt_BR
dc.contributor.authorGouvea, Iuri Ept_BR
unicamp.authorLeticia M Zanphorlin, Departamento de Orgânica, Instituto de Química, UNICAMP, 13083-970 Campinas, Brazil.pt_BR
unicamp.author.externalDébora N Okamoto, Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalMarcia Y Kondo, Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalLilian C G Oliveira, Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalRodrigo V Honorato, Laboratório Nacional de Biociências, Centro Nacional de Pesquisas em Energia e Materiais, 13083-100 Campinas, SP, Brazil.pt
unicamp.author.externalMonika A Coronado, Departamento de Física, IBILCE, UNESP, 15054-000 São José do Rio Preto, Brazil.pt
unicamp.author.externalMariana S Araújo, Departamento de Bioquímica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalGuacyara da Motta, Departamento de Bioquímica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalCamila L Veronez, Departamento de Bioquímica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalSheila S Andrade, Departamento de Ginecologia, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalPaulo S L Oliveira, Laboratório Nacional de Biociências, Centro Nacional de Pesquisas em Energia e Materiais, 13083-100 Campinas, SP, Brazil.pt
unicamp.author.externalRaghuvir K Arni, Departamento de Física, IBILCE, UNESP, 15054-000 São José do Rio Preto, Brazil.pt
unicamp.author.externalAdelia C O Cintra, Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto-USP, 14040-903 Ribeirão Preto, SP, Brazil.pt
unicamp.author.externalSuely V Sampaio, Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto-USP, 14040-903 Ribeirão Preto, SP, Brazil.pt
unicamp.author.externalMaria A Juliano, Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalLuiz Juliano, Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil.pt
unicamp.author.externalMário T Murakami, Laboratório Nacional de Biociências, Centro Nacional de Pesquisas em Energia e Materiais, 13083-100 Campinas, SP, Brazil. Electronic address: mario.murakami@lnbio.cnpem.br.pt
unicamp.author.externalIuri E Gouvea, Departamento de Biofísica, Universidade Federal de São Paulo, 04044-020 São Paulo, SP, Brazil. Electronic address: iurig@yahoo.com.pt
dc.subjectAmino Acid Sequencept_BR
dc.subjectAnimalspt_BR
dc.subjectBothropspt_BR
dc.subjectCrotalid Venomspt_BR
dc.subjectHydrolysispt_BR
dc.subjectKallikreinspt_BR
dc.subjectKineticspt_BR
dc.subjectMetalloproteasespt_BR
dc.subjectMolecular Dynamics Simulationpt_BR
dc.subjectPeptidespt_BR
dc.subjectRadioimmunoassaypt_BR
dc.subjectSerine Endopeptidasespt_BR
dc.subjectSubstrate Specificitypt_BR
dc.subjectFret Peptidespt_BR
dc.subjectKininogenase Activitypt_BR
dc.subjectMolecular Dynamics Simulationspt_BR
dc.subjectSnake Venom Metalloproteinasept_BR
dc.subjectSubstrate Specificitypt_BR
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.en
dc.relation.ispartofBiochimica Et Biophysica Actapt_BR
dc.relation.ispartofabbreviationBiochim. Biophys. Actapt_BR
dc.date.issued2014-Marpt_BR
dc.identifier.citationBiochimica Et Biophysica Acta. v. 1844, n. 3, p. 545-52, 2014-Mar.pt_BR
dc.language.isoengpt_BR
dc.description.volume1844pt_BR
dc.description.firstpage545-52pt_BR
dc.rightsfechadopt_BR
dc.rights.holderCopyright © 2014 Elsevier B.V. All rights reserved.pt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn0006-3002pt_BR
dc.identifier.doi10.1016/j.bbapap.2013.12.014pt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/24373874pt_BR
dc.date.available2015-11-27T13:41:42Z-
dc.date.accessioned2015-11-27T13:41:42Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T13:41:42Z (GMT). No. of bitstreams: 1 pmed_24373874.pdf: 745314 bytes, checksum: 46ee7bbbecb336c7427312ebe1e398b6 (MD5) Previous issue date: 2014en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/201062-
dc.identifier.idPubmed24373874pt_BR
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