Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii

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dc.contributor.authorMoro, Luigi P.
dc.contributor.authorCabral, Hamilton
dc.contributor.authorOkamoto, Débora Noma [UNIFESP]
dc.contributor.authorHirata, Izaura Yoshico [UNIFESP]
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorBonilla-Rodriguez, Gustavo Orlando
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:31:27Z
dc.date.available2016-01-24T14:31:27Z
dc.date.issued2013-04-01
dc.description.abstractMiliin is a serine protease purified from the latex of Euphorbia milii. This work reports the effect of pH and temperature on the catalytic activity of miliin, using fluorescence resonance energy transfer (FRET) substrates. Miliin displayed the highest activity at pH 9 and 35 degrees C. Subsite mapping shows that subsites S-2 to S-2' prefer uncharged residues. the S-2 subsite prefers hydrophobic aliphatic amino acids (Val, Pro and Ile) and defines the cleavage site. This work is the first one that reports subsite mapping of Euphorbiacea proteases. the N-terminal sequence showed higher similarity (40%) with the serine protease LIM9 isolated from Lilium. the presence of Tyr, Pro and Lys at positions 2, 5 and 10 respectively, were observed for most of the serine proteases used for comparison. the N-terminal sequence has striking differences with those reported previously for milin and eumiliin, other serine proteases isolated from the latex of E. milii. (C) 2013 Elsevier B.V. All rights reserved.en
dc.description.affiliationState Univ São Paulo, IBILCE UNESP, Sao Jose Do Rio Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, USP, BR-14049 Ribeirao Preto, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, UNIFESP, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, UNIFESP, EPM, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent633-637
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2013.02.017
dc.identifier.citationProcess Biochemistry. Oxford: Elsevier B.V., v. 48, n. 4, p. 633-637, 2013.
dc.identifier.doi10.1016/j.procbio.2013.02.017
dc.identifier.fileWOS000320413900012.pdf
dc.identifier.issn1359-5113
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/36110
dc.identifier.wosWOS:000320413900012
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofProcess Biochemistry
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectEuphorbia miliien
dc.subjectMiliinen
dc.subjectSubsite mappingen
dc.subjectSerine proteaseen
dc.subjectPlant proteaseen
dc.subjectFRET substratesen
dc.titleCharacterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia miliien
dc.typeinfo:eu-repo/semantics/article
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