Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/31807
Full metadata record
DC FieldValueLanguage
dc.contributor.authorCunha, Carlos Eduardo L. [UNIFESP]
dc.contributor.authorMagliarelli, Helena de Fatima [UNIFESP]
dc.contributor.authorPaschoalin, Thaysa [UNIFESP]
dc.contributor.authorNchinda, Aloysius T.
dc.contributor.authorLima, Jackson C. [UNIFESP]
dc.contributor.authorJuliano, Maria A. [UNIFESP]
dc.contributor.authorPaiva, Paulo B. [UNIFESP]
dc.contributor.authorSturrock, Edward D.
dc.contributor.authorTravassos, Luiz R. [UNIFESP]
dc.contributor.authorCarmona, Adriana K. [UNIFESP]
dc.date.accessioned2016-01-24T13:58:44Z-
dc.date.available2016-01-24T13:58:44Z-
dc.date.issued2009-09-01
dc.identifierhttp://dx.doi.org/10.1515/BC.2009.105
dc.identifier.citationBiological Chemistry. Berlin: Walter de Gruyter & Co, v. 390, n. 9, p. 931-940, 2009.
dc.identifier.issn1431-6730
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/31807-
dc.description.abstractDipeptidyl carboxypeptidase from Escherichia coli (EcDcp) is a zinc metallopeptidase with catalytic properties closely resembling those of angiotensin I-converting enzyme (ACE). However, EcDcp and ACE are classified in different enzyme families (M3 and M2, respectively) due to differences in their primary sequences. We cloned and expressed EcDcp and studied in detail the enzyme's S(3) to S(1)' substrate specificity using positional-scanning synthetic combinatorial (PS-SC) libraries of fluorescence resonance energy transfer (FRET) peptides. These peptides contain ortho-aminobenzoic acid (Abz) and 2,4-dinitrophenyl (Dnp) as donor/acceptor pair. in addition, using FRET substrates developed for ACE [Abz-FRK(Dnp)P-OH, Abz-SDK(Dnp)P-OH and Abz-LFK(Dnp)-OH] as well as natural ACE substrates (angiotensin I, bradykinin, and Ac-SDKP-OH), we show that EcDcp has catalytic properties very similar to human testis ACE. EcDcp inhibition studies were performed with the ACE inhibitors captopril (K(i) = 3 nM) and lisinopril (K(i) = 4.4 mu M) and with two C-domain-selective ACE inhibitors, 5-S-5-benzamido-4-oxo-6-phenylhexanoyl-L-tryptophan (kAW; K(i) = 22.0 mu M) and lisinopril-Trp (K(i) = 0.8 nM). Molecular modeling was used to provide the basis for the differences found in the inhibitors potency. the phylogenetic relationship of EcDcp and related enzymes belonging to the M3 and M2 families was also investigated and the results corroborate the distinct origins of EcDcp and ACE.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipWellcome Trust, UK
dc.description.sponsorshipNational Research Foundation
dc.format.extent931-940
dc.language.isoeng
dc.publisherWalter de Gruyter & Co
dc.relation.ispartofBiological Chemistry
dc.rightsAcesso restrito
dc.subjectangiotensin I-converting enzymeen
dc.subjectdipeptidyl carboxypeptidaseen
dc.subjectinhibitorsen
dc.subjectmolecular modelingen
dc.subjectphylogenyen
dc.subjectspecificity studiesen
dc.titleCatalytic properties of recombinant dipeptidyl carboxypeptidase from Escherichia coli: a comparative study with angiotensin I-converting enzymeen
dc.typeArtigo
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Cape Town
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniv Cape Town, Div Med Biochem, Inst Infect Dis & Mol Med, ZA-7925 Cape Town, South Africa
dc.description.affiliationUniversidade Federal de São Paulo, Dept Informat Technol Hlth, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Informat Technol Hlth, BR-04023062 São Paulo, Brazil
dc.identifier.doi10.1515/BC.2009.105
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000269485600012
Appears in Collections:Em verificação - Geral

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.