• It contains inhibitors of multiple cysteine and serine protease families. (wikipedia.org)
  • This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. (thermofisher.com)
  • USP40 has several biochemical functions, for example, cysteine-type endopeptidase activity, ubiquitin-specific protease activity. (creativebiomart.net)
  • The CRCBT-02-001 monoclonal antibody specifically binds to human CD364 which is also known as Peptidase inhibitor 16 (PI-16) or Protease inhibitor 16. (bdbiosciences.com)
  • The cystatin superfamily of cysteine protease inhibitors is composed of distinct families of intracellular stefins and secreted true cystatins. (bvsalud.org)
  • Predicted to allow carboxypeptidase activity and cysteine-type endopeptidase activity. (enigmadiagnostics.com)
  • Orthologous to human USP1 (ubiquitin specific peptidase 1). (zfin.org)
  • The peptidase inhibitor I9 family contains the propeptide domain at the N-terminus of peptidases belonging to MEROPS family S8A, subtilisins . (wikipedia.org)
  • We determined that FhCyLS-2 is a broad specificity inhibitor of cysteine cathepsins from both the host and F. hepatica, suggesting a dual role in the regulation of exogenous and endogenous proteolysis. (bvsalud.org)
  • Pyroglutamyl peptidase-1 (PGPEP-1) is an omega peptidase which removes pyroglutamyl residues from the amino termini of peptides and proteins (1). (novusbio.com)
  • Moreover, the relative orientation of these catalytic residues is similar to that observed in the analogous Ser-His-His triad, a variant of the classic Ser-His-Asp charge relay system, suggesting the convergent evolution of a catalytic mechanism in quite distinct peptidase families. (rcsb.org)
  • The subdomains are in the opposite order to those found in peptidases from clan CA, and this is reflected in the order of active site residues: His/Asn/Gln/Cys. (embl.de)
  • PPT1, which removes fatty acyl groups from cysteine residues on fatty-acid modified proteins, remains in the endoplasmic reticulum, where it is inactive, causing saposins A and D to accumulate in the lysosomes. (medscape.com)
  • This is a group of cysteine peptidases which constitute MEROPS peptidase family C54 (Aut2 peptidase family, clan CA), which are a group of proteins of unknown function. (embl.de)
  • The active site features a novel Cys-His-His catalytic triad that appears to be a unique structural signature of this cysteine peptidase family. (rcsb.org)
  • Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (embl.de)
  • Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad. (rostlab.org)
  • Cathepsin K, a member of a large family of cysteine peptidases, is an enzyme that breaks down the collagen bone matrix as part of a normal biological process. (bioworld.com)
  • The immunosensor showed a detection limit of 13.0 nmol L-1 with excellent specificity, showing no response for different proteins that include another cysteine peptidase that is used as a target to detect Xylella fastidiosa bacterium, responsible for another important citrus disease. (eppo.int)
  • and dipeptidyl peptidase, a human enzyme involved in type 2 diabetes - for their ability to inhibit Mpro or PLpro. (worldpharmanews.com)
  • The human ATG4D gene encodes the protein Autophagy related 4D, cysteine peptidase. (wikipedia.org)
  • It is a member of the cysteine-rich secretory protein (CRISP) family and is likewise known as CRISP9. (bdbiosciences.com)
  • The protein encoded by this gene is a lysosomal cysteine proteinase and a member of the C1 peptidase family. (enigmadiagnostics.com)
  • Peptidases are enzymes with diverse functionality and perform important tasks in peptide degradation, pathogenic defense, or regulation in cellular pathways. (uni-bayreuth.de)
  • Since it is beyond the scope of the Guide to list all peptidase and proteinase activities, this summary focuses on selected enzymes of significant pharmacological interest that have ligands (mostly small-molecules) directed against them. (guidetoimmunopharmacology.org)
  • Predicted to enable cysteine-type deubiquitinase activity. (zfin.org)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (embl.de)
  • Macroautophagy in Leishmania, which is important for the cellular remodeling required during differentiation, relies upon the hydrolytic activity of two ATG4 cysteine peptidases (ATG4.1 and ATG4.2). (strath.ac.uk)
  • Patients with CLN2 NCL are deficient in a pepstatin-insensitive lysosomal peptidase called tripeptidyl peptidase 1 (TTP1). (medscape.com)
  • Proteinase propeptide inhibitors (sometimes referred to as activation peptides) are responsible for the modulation of folding and activity of the peptidase pro-enzyme or zymogen . (wikipedia.org)
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (embl.de)
  • In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. (embl.de)
  • Belongs to peptidase family C14. (lu.se)
  • Peptidases in the clan hydrolyse and transfer bacterial cell wall peptides. (embl.de)
  • A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. (embl.de)
  • However, the reason for a concerted mechanism in serine peptidases is poorly understood. (uni-bayreuth.de)
  • At first I investigated the mechanism of a cysteine peptidase, which we also characterized in the laboratory. (uni-bayreuth.de)
  • the E-value for the Peptidase_C54 domain shown below is 2.3e-39. (embl.de)
  • Contrary to this, I found a negative potential within serine peptidases. (uni-bayreuth.de)
  • In addition to that, the active site geometry of serine peptidases has to be compact to allow for the simultaneous events of proton transfer to histidine and nucleophilic attack. (uni-bayreuth.de)
  • Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. (embl.de)
  • Analysis of protonation characteristics showed, that such a negative potential in serine peptidases is essential to enhance the basicity of the catalytic histidine, which facilitates proton acceptance from serine. (uni-bayreuth.de)