Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L

Recombinant human cathepsin X is a carboxymonopeptidase only: a comparison with cathepsins B and L

Autor Puzer, L. Google Scholar
Cotrin, S. S. Google Scholar
Cezari, MHS Google Scholar
Hirata, I. Y. Google Scholar
Juliano, M. A. Google Scholar
Stefe, L. Google Scholar
Turk, D. Google Scholar
Turk, B. Google Scholar
Juliano, L. Google Scholar
Carmona, A. K. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Jozef Stefan Inst
Resumo 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.
Palavra-chave carboxymonopeptidase
cathepsin B
cathepsin L
cathepsin X
lysosomal cathepsins
selective substrate
specificity studies
Idioma Inglês
Data de publicação 2005-11-01
Publicado em Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 386, n. 11, p. 1191-1195, 2005.
ISSN 1431-6730 (Sherpa/Romeo, fator de impacto)
Publicador Walter de Gruyter & Co
Extensão 1191-1195
Fonte http://dx.doi.org/10.1515/BC.2005.136
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000233703800013
Endereço permanente http://repositorio.unifesp.br/handle/11600/28547

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