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

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

Autor Moro, Luigi P. Google Scholar
Cabral, Hamilton Google Scholar
Okamoto, Débora Noma Autor UNIFESP Google Scholar
Hirata, Izaura Yoshico Autor UNIFESP Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Bonilla-Rodriguez, Gustavo Orlando Google Scholar
Instituição Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo Miliin 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.
Palavra-chave Euphorbia milii
Miliin
Subsite mapping
Serine protease
Plant protease
FRET substrates
Idioma Inglês
Financiador Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
Data de publicação 2013-04-01
Publicado em Process Biochemistry. Oxford: Elsevier B.V., v. 48, n. 4, p. 633-637, 2013.
ISSN 1359-5113 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 633-637
Fonte http://dx.doi.org/10.1016/j.procbio.2013.02.017
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000320413900012
Endereço permanente http://repositorio.unifesp.br/handle/11600/36110

Exibir registro completo




Arquivo

Nome: WOS000320413900012.pdf
Tamanho: 457.8KB
Formato: PDF
Descrição:
Abrir arquivo

Este item está nas seguintes coleções

Buscar


Navegar

Minha conta