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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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]
Total Authors: 7
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: Applied Biochemistry and Biotechnology; v. 187, n. 4, p. 1158-1172, APR 2019.
Web of Science Citations: 1
Abstract

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)

FAPESP's process: 11/06986-0 - Determination of the specificity of peptidases isolated from fungi using fluorescence resonance energy transfer (FRET) peptides as substrates
Grantee:Hamilton Cabral
Support Opportunities: Regular Research Grants
FAPESP's process: 12/24703-8 - Proteomics analyses of meso and thermophilic filamentous fungi exposed to physical and chemical factors
Grantee:Hamilton Cabral
Support Opportunities: Regular Research Grants