dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.contributorJozef Stefan Inst
dc.creatorPuzer, L.
dc.creatorCotrin, S. S.
dc.creatorCezari, MHS
dc.creatorHirata, I. Y.
dc.creatorJuliano, M. A.
dc.creatorStefe, L.
dc.creatorTurk, D.
dc.creatorTurk, B.
dc.creatorJuliano, L.
dc.creatorCarmona, A. K.
dc.date.accessioned2016-01-24T12:38:09Z
dc.date.accessioned2022-10-07T21:24:39Z
dc.date.available2016-01-24T12:38:09Z
dc.date.available2022-10-07T21:24:39Z
dc.date.created2016-01-24T12:38:09Z
dc.date.issued2005-11-01
dc.identifierBiological Chemistry. Berlin: Walter de Gruyter & Co, v. 386, n. 11, p. 1191-1195, 2005.
dc.identifier1431-6730
dc.identifierhttp://repositorio.unifesp.br/handle/11600/28547
dc.identifier10.1515/BC.2005.136
dc.identifierWOS:000233703800013
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/4029192
dc.description.abstractThe S-1 and S-2 subsite specificity of recombinant human cathepsins X was studied using fluorescence resonance energy transfer (FRET) peptides with the general sequences Abz-Phe-Xaa-Lys(Dnp)-OH and Abz-XaaArg-Lys(Dnp)-OH, respectively (Abz=ortho-aminobenzoic acid and Dnp=2,4-dinitrophenyl; Xaa=various amino acids). Cathepsin X cleaved all substrates exclusively as a carboxymonopeptidase and exhibited broad specificity. for comparison, these peptides were also assayed with cathepsins B and L. Cathepsin L hydrolyzed the majority of them with similar or higher catalytic efficiency than cathepsin X, acting as an endopeptidase mimicking a carboxymonopepticlase (pseudo-carboxymonopeptidase). in contrast, cathepsin B exhibited poor catalytic efficiency with these substrates, acting as a carboxydipeptidase or an endopeptidase. the S-1' subsite of cathepsin X was mapped with the peptide series AbzPhe-Arg-Xaa-OH and the enzyme preferentially hydrolyzed substrates with hydrophobic residues in the P-1' position.
dc.languageeng
dc.publisherWalter de Gruyter & Co
dc.relationBiological Chemistry
dc.rightsAcesso restrito
dc.subjectcarboxymonopeptidase
dc.subjectcathepsin B
dc.subjectcathepsin L
dc.subjectcathepsin X
dc.subjectlysosomal cathepsins
dc.subjectselective substrate
dc.subjectspecificity studies
dc.titleRecombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L
dc.typeArtigo


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