Analysis of peptidase activities of a cathepsin B-like (TcoCBc1) from Trypanosoma congolense

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dc.contributor.author Oliveira, Lilian C. G. [UNIFESP]
dc.contributor.author Okamoto, Debora N. [UNIFESP]
dc.contributor.author Oliveira, Juliana R. [UNIFESP]
dc.contributor.author Kondo, Marcia Y. [UNIFESP]
dc.contributor.author Gouvea, Iuri E. [UNIFESP]
dc.contributor.author Biteau, Nicolas
dc.contributor.author Baltz, Theo
dc.contributor.author Murakami, Mario T.
dc.contributor.author Juliano, Luiz [UNIFESP]
dc.contributor.author Juliano, Maria A. [UNIFESP]
dc.date.accessioned 2016-01-24T14:37:31Z
dc.date.available 2016-01-24T14:37:31Z
dc.date.issued 2014-07-01
dc.identifier http://dx.doi.org/10.1016/j.bbapap.2014.04.001
dc.identifier.citation Biochimica Et Biophysica Acta-proteins and Proteomics. Amsterdam: Elsevier B.V., v. 1844, n. 7, p. 1260-1267, 2014.
dc.identifier.issn 1570-9639
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/37933
dc.description.abstract The substrate specificity of TcoCBc1 was evaluated using two internally quenched fluorescent peptide libraries with randomized sequences designed to detect carboxydipeptidase (Abz-GXXZXK(Dnp)-OH) and endopeptidase (Abz-GXXZXXQ-EDDnp) activities at acidic and neutral pHs, respectively. All the data obtained with TcoCBc1 were compared with those of human cathepsin B, including the pH profiles of the hydrolytic reactions. the most relevant observation is the preference of TcoCBc1 for substrates with a pair of acidic amino acids at positions P-2 and P-1 for its carboxydipeptidase activity and the well acceptance for E and D at P-1 position for endopeptidase activity. These peculiar preferences for negatively charged groups of TcoCBc1 and its requirements for carboxydipeptidase activity were also observed on Abz labeled analogues of bradykinin (Abz-RPPG(down arrow)FSAFR-OH, Abz-RPPG(down arrow)FS(down arrow)AF-OH, Abz-RPPG(down arrow)DE(down arrow)AF-OH) and angiotensin I (Abz-DR(down arrow)VYIHAFHL-OH), where l indicates the cleavage site. TcoCBc1 was modeled based on the atomic coordinates of the cathepsin B from Trypanosoma brucei and the positively charged environment in TcoCBc1 catalytic site contrasts with the negatively charged environment in human cathepsin B. the preferences of S-1 and S-2 subsites of TcoCBc1 for acidic amino acids have to be taken into consideration for future studies of physiological roles of TcoCBc1 as for instance in apoptotic processes of Trypanosoma congolense. (C) 2014 Elsevier B.V. All rights reserved. en
dc.description.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorship Instituto Nacional de Fluidos Complexos (INCT-FCx-Project)
dc.format.extent 1260-1267
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Biochimica Et Biophysica Acta-proteins and Proteomics
dc.rights Acesso restrito
dc.subject Protease en
dc.subject Peptide library en
dc.subject Fluorescent substrate en
dc.subject Carboxydipeptidase en
dc.subject Endopeptidase en
dc.title Analysis of peptidase activities of a cathepsin B-like (TcoCBc1) from Trypanosoma congolense en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Bordeaux Segalen
dc.contributor.institution Ctr Nacl Pesquisas Energia & Mat
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-0444040 São Paulo, Brazil
dc.description.affiliation Univ Bordeaux Segalen, CNRS, UMR 5234, F-33000 Bordeaux, France
dc.description.affiliation Ctr Nacl Pesquisas Energia & Mat, Lab Nacl Biociencias, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-0444040 São Paulo, Brazil
dc.description.sponsorshipID FAPESP: 12/50191-4R
dc.description.sponsorshipID CNPq: 471340/2011-1
dc.description.sponsorshipID CNPq: 470388/2010-2
dc.description.sponsorshipID Instituto Nacional de Fluidos Complexos (INCT-FCx-Project): 573560/2008-0
dc.identifier.doi 10.1016/j.bbapap.2014.04.001
dc.description.source Web of Science
dc.identifier.wos WOS:000337211100010



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