Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L
dc.contributor | Universidade Federal de São Paulo (UNIFESP) | |
dc.contributor | Jozef Stefan Inst | |
dc.creator | Puzer, L. | |
dc.creator | Cotrin, S. S. | |
dc.creator | Cezari, MHS | |
dc.creator | Hirata, I. Y. | |
dc.creator | Juliano, M. A. | |
dc.creator | Stefe, L. | |
dc.creator | Turk, D. | |
dc.creator | Turk, B. | |
dc.creator | Juliano, L. | |
dc.creator | Carmona, A. K. | |
dc.date.accessioned | 2016-01-24T12:38:09Z | |
dc.date.accessioned | 2022-10-07T21:24:39Z | |
dc.date.available | 2016-01-24T12:38:09Z | |
dc.date.available | 2022-10-07T21:24:39Z | |
dc.date.created | 2016-01-24T12:38:09Z | |
dc.date.issued | 2005-11-01 | |
dc.identifier | Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 386, n. 11, p. 1191-1195, 2005. | |
dc.identifier | 1431-6730 | |
dc.identifier | http://repositorio.unifesp.br/handle/11600/28547 | |
dc.identifier | 10.1515/BC.2005.136 | |
dc.identifier | WOS:000233703800013 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/4029192 | |
dc.description.abstract | The 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.language | eng | |
dc.publisher | Walter de Gruyter & Co | |
dc.relation | Biological Chemistry | |
dc.rights | Acesso restrito | |
dc.subject | carboxymonopeptidase | |
dc.subject | cathepsin B | |
dc.subject | cathepsin L | |
dc.subject | cathepsin X | |
dc.subject | lysosomal cathepsins | |
dc.subject | selective substrate | |
dc.subject | specificity studies | |
dc.title | Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L | |
dc.type | Artigo |