ArticleThe Biochemical journal2003
S3 to S3' subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 57 citations in OpenAlex.
- Predicting Structural Susceptibility of Proteins to Proteolytic Processing.International journal of molecular sciences · 2023Article
- Structure determinants defining the specificity of papain-like cysteine proteases.Computational and structural biotechnology journal · 2022Review
- Molecular probes for selective detection of cysteine cathepsins.Organic & biomolecular chemistry · 2021Review
- Predictive models of protease specificity based on quantitative protease-activity profiling data.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- Computational predictions of cysteine cathepsin-mediated fibrinogen proteolysis.Protein science : a publication of the Protein Society · 2018Article
- Emerging challenges in the design of selective substrates, inhibitors and activity-based probes for indistinguishable proteases.The FEBS journal · 2017Review
- Highly sensitive and adaptable fluorescence-quenched pair discloses the substrate specificity profiles in diverse protease families.Scientific reports · 2017Article
- Dissecting the active site of the collagenolytic cathepsin L3 protease of the invasive stage of Fasciola hepatica.PLoS neglected tropical diseases · 2013Article
- Cysteine cathepsins: from structure, function and regulation to new frontiers.Biochimica et biophysica acta · 2012Review
- Structural determinants of limited proteolysis.Journal of proteome research · 2011Article
- A modeling study of aldehyde inhibitors of human cathepsin K using partial least squares method.Research in pharmaceutical sciences · 2011Article
- Molecular dynamics simulations of the catalytic pathway of a cysteine protease: a combined QM/MM study of human cathepsin K.Journal of the American Chemical Society · 2007Article
- Cathepsin K: a cysteine protease with unique kinin-degrading properties.The Biochemical journal · 2004Article
- Cyclic, linear, cycloretro-isomer, and cycloretro-inverso peptides derived from the C-terminal sequence of bradykinin as substrates or inhibitors of serine and cysteine proteases.The protein journal · 2004Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
We have systematically examined the S3 to S3' subsite substrate specificity requirements of cathepsin K using internally quenched fluorescent peptides derived from the lead sequence Abz-KLRFSKQ-EDDnp [where Abz is o -aminobenzoic acid and EDDnp is N -(2,4-dinitrophenyl)ethylenediamine]. We assayed six series of peptides, in which each position except Gln was substituted with various natural amino acids. The results indicated that the S3-S1 subsite requirements are more restricted than those of S1'-S3'. Cathepsin K preferentially accommodates hydrophobic amino acids with aliphatic side chains (Leu, Ile and Val) in the S2 site. Modifications at P1 residues also have a large influence on cathepsin K activity. Positively charged residues (Arg and Lys) represent the best accepted amino acids in this position, although a particular preference for Gly was found as well. Subsite S3 accepted preferentially basic amino acids such as Lys and Arg. A broad range of amino acids was accommodated in the remaining subsites. We further explored the acceptance of a Pro residue in the P2 position by cathepsin K in order to develop specific substrates for the enzyme. Two series of peptides with the general sequences Abz-KXPGSKQ-EDDnp and Abz-KPXGSKQ-EDDnp (where X denotes the position of the amino acid that is altered) were synthesized. The substrates Abz-KPRGSKQ-EDDnp and Abz-KKPGSKQ-EDDnp were cleaved by cathepsin K at the Arg-Gly and Gly-Ser bonds respectively, and have been shown to be specific for cathepsin K when compared with other lysosomal cysteine proteases such as cathepsins L and B and with the aspartyl protease cathepsin D.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.