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

Author 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
Institution Universidade Federal de São Paulo (UNIFESP)
Jozef Stefan Inst
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.
Keywords carboxymonopeptidase
cathepsin B
cathepsin L
cathepsin X
lysosomal cathepsins
selective substrate
specificity studies
Language English
Date 2005-11-01
Published in Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 386, n. 11, p. 1191-1195, 2005.
ISSN 1431-6730 (Sherpa/Romeo, impact factor)
Publisher Walter de Gruyter & Co
Extent 1191-1195
Access rights Closed access
Type Article
Web of Science ID WOS:000233703800013

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