Biochemical Properties and Catalytic Specificity of a Novel Neutral Serine Peptidase Secreted by Fungus Pyrenochaetopsis sp.

Autor(es)

da Silva, Ronivaldo Rodrigues ^[1] ; da Rosa, Nathalia Gonsales ^[2] ; Goncalves de Oliveira, Lilian Caroline ^[3] ; Juliano, Maria Aparecida ^[3] ; Juliano, Luiz ^[3] ; Rosa, Jose C. ^[4] ; Cabral, Hamilton ^[2]

Afiliação do(s) autor(es)

^[1] Univ Estadual Paulista, Inst Biociencias Letras & Ciencias Exatas, Sao Jose Do Rio Preto, SP - Brazil

^[2] Univ Sao Paulo, Fac Ciencias Farmaceut Ribeirao Preto, Av Cafe S-N, Campus Univ, BR-14040903 Ribeirao Preto, SP - Brazil

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

^[4] Univ Sao Paulo, Fac Med Ribeirao Preto, Ribeirao Preto, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Applied Biochemistry and Biotechnology; v. 187, n. 4, p. 1158-1172, APR 2019.
• Citações Web of Science: 1

Resumo

The fungal genus Pyrenochaetopsis has received particular attention because of its different lifestyles, such as numerous plant pathogenic, saprophytic, and endophytic species. Its ability to infect plant cells relies heavily upon secreted peptidases. Here, we investigated the biochemical properties and catalytic specificity of a new serine peptidase secreted by the filamentous fungus Pyrenochaetopsis sp. We found that while this neutral serine peptidase displayed optimal activity at a pH of 7.0 and temperature of 45 degrees C, it tolerated a wide range of pH conditions and temperatures lower than 45 degrees C. Its peptidase activity was depressed by some metallic ions (such as aluminum, cobalt, and copper (II) chloride) and enhanced by others (such as sodium, lithium, magnesium, potassium, calcium, and manganese). Lastly, the enzyme showed the greatest specificity for non-polar amino acids, particularly leucine and isoleucine, and moderate specificity for basic and neutral polar amino acids. It displayed the least specificity for acidic residues. (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
• Processo FAPESP: 12/24703-8 - Análises proteômicas de fungos filamentosos meso e termofílicos expostos aos fatores físico e químico
• Beneficiário: Hamilton Cabral
• Modalidade de apoio: Auxílio à Pesquisa - Regular