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Screening and characterization of serine carboxyl peptidases and glutamic peptidases in bacteria isolated from the composting operation at the São Paulo Zoo Park

Grant number: 13/12106-8
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): September 01, 2013
Effective date (End): August 31, 2015
Field of knowledge:Biological Sciences - Biochemistry - Enzymology
Principal researcher:Maria Aparecida Juliano
Grantee:Márcia Yuri Kondo
Home Institution: Instituto Nacional de Farmacologia (INFAR). Universidade Federal de São Paulo (UNIFESP). Campus São Paulo. São Paulo , SP, Brazil
Associated research grant:12/50191-4 - Synthesis, kinetic studies and applications of substrates and inhibitors for proteolytic enzymes, AP.TEM

Abstract

Proteolytic enzymes are widespread in all organisms and are involved in a wide range of biological roles. There are seven distinct classes of proteases (serine-, cysteine-, aspartate-, metallo-, threonine-, glutamic peptidase and asparagine peptide lyases), grouped according to their catalytic mechanism. The main groups of carboxylic proteases which are catalytically active at acidic pH are aspartic peptidases, serine carboxyl peptidases and glutamic peptidases. Whereas aspartic peptidases are well known and studied, the other two groups are relatively new and there is lack of information about them. Serine carboxyl peptidases are single domain proteins resembling the structure of the serine peptidase subtilisin and their catalytic triad is composed by the side chains of serine, glutamic acid and aspartic acid (S-E-D). They are widespread among several organisms, being found especially in bacteria. Glutamic peptidases have catalytic dyad composed by glutamic acid and glutamine (E-Q) and a tertiary structure formed by a b-sandwich of antiparallel b-sheets. So far, most of glutamic peptidases were isolated from fungi, besides their existence in bacteria. The aim of this project is to screen, isolate and characterize new serine carboxyl peptidases and glutamic peptidases exploring the collection of bacteria, which grow in acidic pH, that were isolated from the composting operation at the São Paulo Zoo Park as well as construct recombinant expression systems for these proteases. The discovery of new proteases from these groups in bacteria will provide important basic information and possible biotechnological applications.

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
KONDO, MARCIA Y.; GOUVEA, IURI E.; OKAMOTO, DEBORA N.; SANTOS, JORGE A. N.; SOUCCAR, CADEN; ODA, KOHEI; JULIANO, LUIZ; JULIANO, MARIA A.. Analysis of catalytic properties of tripeptidyl peptidase I (TTP-I), a serine carboxyl lysosomal protease, and its detection in tissue extracts using selective FRET peptide substrate. Peptides, v. 76, p. 80-86, . (13/12106-8, 12/50191-4)
RAMOS, PATRICIA L.; KONDO, MARCIA Y.; SANTOS, SAARA M. B.; DE VASCONCELLOS, SUZAN P.; ROCHA, RAFAEL C. S.; DA CRUZ, JOAO B.; EUGENIO, PATRICIA F. M.; CABRAL, HAMILTON; JULIANO, MARIA A.; JULIANO, LUIZ; et al. A Tropical Composting Operation Unit at SAo Paulo Zoo as a Source of Bacterial Proteolytic Enzymes. Applied Biochemistry and Biotechnology, v. 187, n. 1, p. 282-297, . (14/07037-0, 12/50191-4, 13/12106-8, 11/06548-2)

Please report errors in scientific publications list by writing to: cdi@fapesp.br.

Filed patent(s) as a result of this research project

MÉTODO DE IDENTIFICAÇÃO DE COMPOSTOS ANTIVIRAIS, COMPOSTOS ANTIVIRAIS, MÉTODO DE AVALIAÇÃO DA FUNCIONALIDADE DOS COMPOSTOS ANTIVIRAIS, USO DOS COMPOSTOS ANTIVIRAIS E COMPOSIÇÃO FARMACÊUTICA ANTIVIRAL BR1020150065612 - Universidade de São Paulo (USP) ; Universidade Federal de São Paulo (UNIFESP) . Antonia Tavares do Amaral; Erika Piccirillo; Maria Aparecida Juliano; Marcia Yuri Kondo - March 2015, 24