The Identification and Biochemical Properties of the Catalytic Specificity of a Serine Peptidase Secreted by Aspergillus fumigatus Fresenius

Autor(es)

da Silva, Ronivaldo Rodrigues ^[1] ; Caetano, Renato Cesar ^[2] ; Okamoto, Debora Nona ^[3] ; Gonalves de Oliveira, Lilian Caroline ^[3] ; Bertolin, Thiago Carlos ^[3] ; Juliano, Maria Aparecida ^[3] ; Juliano, Luiz ^[3] ; de Oliveira, Arthur H. C. ^[4] ; Rosa, Jose C. ^[5] ; Cabral, Hamilton ^[2]

Afiliação do(s) autor(es)

^[1] Univ Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas, Sao Paulo - Brazil

^[2] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Sao Paulo - Brazil

^[3] Univ Fed Sao Paulo, UNIFESP, Sao Paulo - Brazil

^[4] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Ribeirao Preto, SP - Brazil

^[5] Univ Sao Paulo, Fac Med Ribeirao Preto, Ribeirao Preto, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: PROTEIN AND PEPTIDE LETTERS; v. 21, n. 7, p. 663-671, 2014.
• Citações Web of Science: 14

Resumo

Aspergillus fumigatus is a saprophytic fungus as well as a so-called opportunist pathogen. Its biochemical potential and enzyme production justify intensive studies about biomolecules secreted by this microorganism. We describe the alkaline serine peptidase production, with optimum activity at 50 degrees C and a pH of 7.5 and a reduction in proteolytic activity in the presence of the Al+3 ions. When using intramolecularly quenched fluorogenic substrates, the highest catalytic efficiency was observed with the amino acid leucine on subsite S' (3) (60,000 mM(-1)s(-1)) and preference to non- polar amino acids on subsite S-3. In general, however, the peptidase shows non- specificity on other subsites studied. According to the biochemical characteristics, this peptidase may be an important biocatalyst for the hydrolysis of an enormous variety of proteins and can constitute an essential molecule for the saprophytic lifestyle or invasive action of the opportunistic pathogen. The peptidase described herein exhibits an estimated molecular mass of 33 kDa. Mass spectrometry analysis identified the sequence GAPWGLGSISHK displaying similarities to that of serine peptidase from Aspergillus fumigatus. These data may lead to a greater understanding of the advantageous biochemical potential, biotechnological interest, and trends of this fungus in spite of being an opportunist pathogen. (AU)

• Processo FAPESP: 11/06986-0 - Determinação da especificidade de peptidases isoladas de fungos usando peptídeos FRET como substratos
• Beneficiário: Hamilton Cabral
• Modalidade de apoio: Auxílio à Pesquisa - Regular