ArticleThe Biochemical journal2002
Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Dipeptide-Derived Alkynes as Potent and Selective Irreversible Inhibitors of Cysteine Cathepsins.Journal of medicinal chemistry · 2023Article
- IQF characterization of a cathepsin B-responsive nanoprobe for report of differentiation of HL60 cells into macrophages.RSC advances · 2021Article
- Asymmetric Disulfanylbenzamides as Irreversible and Selective Inhibitors of Staphylococcus aureus Sortase A.ChemMedChem · 2020Article
- Bispecific Antibodies and Antibody-Drug Conjugates for Cancer Therapy: Technological Considerations.Biomolecules · 2020Review
- New Glutamine-Containing Substrates for the Assay of Cysteine Peptidases From the C1 Papain Family.Frontiers in molecular biosciences · 2020Article
- Activity profiling of peptidases in Angiostrongylus costaricensis first-stage larvae and adult worms.PLoS neglected tropical diseases · 2018Article
- Eliciting unnatural immune responses by activating cryptic epitopes in viral antigens.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Enzyme-Cleavable Polymeric Micelles for the Intracellular Delivery of Proapoptotic Peptides.Molecular pharmaceutics · 2017Article
- Cathepsin B-sensitive polymers for compartment-specific degradation and nucleic acid release.Journal of controlled release : official journal of the Controlled Release Society · 2012Article
- Structural basis for inhibition of cathepsin B drug target from the human blood fluke, Schistosoma mansoni.The Journal of biological chemistry · 2011Article
- Enzymatic degradation of the hydrogels based on synthetic poly(α-amino acid)s.Journal of materials science. Materials in medicine · 2011Article
- Cathepsin B: Basis Sequence: Mouse.The AFCS-nature molecule pages · 2011Article
- Quantifying cathepsin S activity in antigen presenting cells using a novel specific substrate.The Journal of biological chemistry · 2008Article
- Analysis of substrate specificity and endopeptidyl activities of the cathepsin B-like proteinase from Helicoverpa armigera.The protein journal · 2005Article
- S3 to S3' subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates.The Biochemical journal · 2003Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have examined in detail the specificity of the subsites S1, S2, S1' and S2' for the carboxydipeptidase activity of cathepsin B by synthesizing and assaying four series of internally quenched fluorescent peptides based on the sequence Dnp-GFRFW-OH, where Dnp (2,4-dinitrophenyl) is the quenching group of the fluorescence of the tryptophan residue. Each position, except the glycine, was substituted with 15 different naturally occurring amino acids. Based on the results we obtained, we also synthesized efficient and sensitive substrates that contained o -aminobenzoic acid and 3-Dnp-(2,3-diaminopropionic acid), or epsilon-amino-Dnp-Lys, as the fluorescence donor-receptor pair. The higher kinetic parameter values for the carboxydipeptidase compared with the endopeptidase activity of cathepsin B allowed an accurate analysis of its specificity. The subsite S1 accepted preferentially basic amino acids for hydrolysis; however, substrates with phenylalanine and aliphatic side-chain-containing amino acids at P1 had lower K m values. Despite the presence of Glu245 at S2, this subsite presented clear preference for aromatic amino acid residues, and the substrate with a lysine residue at P2 was hydrolysed better than that containing an arginine residue. S1' is essentially a hydrophobic subsite, and S2' has particular preference for phenylalanine or tryptophan residues.
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