ArticleThe Biochemical journal2000
Probing the specificity of cysteine proteinases at subsites remote from the active site: analysis of P4, P3, P2' and P3' variations in extended substrates.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 68 citations in OpenAlex.
- Characterization of a Bacteriocin-like Substance fromVeterinary sciences · 2026Article
- Inhibition of Cathepsin B protects against vandetanib-induced hepato-cardiotoxicity by restoring lysosomal damage.International journal of biological sciences · 2026Article
- 1,2,4-Thiadiazolidin-3,5-Diones as Inhibitors of Cysteine Proteases.Molecules (Basel, Switzerland) · 2025Article
- Plant cathepsin B, a versatile protease.Frontiers in plant science · 2024Review
- Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.Protein science : a publication of the Protein Society · 2022Article
- Novel Cysteine Protease Inhibitor Derived from theToxins · 2021Article
- IQF characterization of a cathepsin B-responsive nanoprobe for report of differentiation of HL60 cells into macrophages.RSC advances · 2021Article
- A Kunitz-type peptide fromThe journal of venomous animals and toxins including tropical diseases · 2020Article
- Purification and Biochemical Characterization of TsMS 3 and TsMS 4: Neuropeptide-Degrading Metallopeptidases in theToxins · 2019Article
- Selective imaging of cathepsin L in breast cancer by fluorescent activity-based probes.Chemical science · 2018Article
- 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
- A multifunctional serine protease primes the malaria parasite for red blood cell invasion.The EMBO journal · 2009Article
- Processing of capsid protein by cathepsin L plays a crucial role in replication of Japanese encephalitis virus in neural and macrophage cells.Journal of virology · 2007Article
- Molecular determinants of substrate specificity for Semliki Forest virus nonstructural protease.Journal of virology · 2006Article
- Analysis of substrate specificity and endopeptidyl activities of the cathepsin B-like proteinase from Helicoverpa armigera.The protein journal · 2005Article
- 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
- Probing cathepsin K activity with a selective substrate spanning its active site.The Biochemical journal · 2003Article
- S3 to S3' subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates.The Biochemical journal · 2003Article
- Cathepsin B carboxydipeptidase specificity analysis using internally quenched fluorescent peptides.The Biochemical journal · 2002Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have determined the kinetic parameters for the hydrolysis by papain, cathepsin B and cathepsin L of internally quenched fluorescent peptides derived from the lead peptides Abz-AAFRSAQ-EDDnp [in which Abz and EDDnp stand for o-aminobenzoic acid and N-(2,4-dinitrophenyl)ethylenediamine respectively], to map the specificity of S(4) and S(3) subsites, and Abz-AFRSAAQ-EDDnp, to identify the specificity of S(2)' and S(3)'. Abz and EDDnp were the fluorescent quencher pair. These two series of peptides were cleaved at the Arg-Ser bond and systematic modifications at P(4), P(3), P(2)' and P(3)' were made. The S(4) to S(2)' subsites had a significant influence on the hydrolytic efficiencies of the three enzymes. Only papain activity was observed to be dependent on S(3)', indicating that its binding site is larger than those of cathepsins B and L. Hydrophobic amino acids were accepted at S(4), S(3), S(2)' and S(3)' of the three enzymes. The best substrates for cathepsins L and B had Trp and Asn at P(2)' respectively; variations at this position were less accepted by these enzymes. The best substrates for papain were peptides containing Trp, Tyr or Asn at P(3)'. Basic residues at P(3) and P(4) were well accepted by cathepsin L and papain. We also explored the susceptibility of substrates Abz-AFRSXAQ-EDDnp, modified at P(2)' (X), to human cathepsin B mutants from which one or two occluding loop contacts had been removed. The modifications at His(111) (H111A) and His(110) (H110A) of cathepsin B led to an increase in k(cat) values of one or two orders of magnitude. The hydrolytic efficiencies of these cathepsin B mutants became closer to those of papain or cathepsin L.
Indexed as
Identifiers
10727410PMC1220939W2141352711What OpenQuestion holds
Registered trials
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.