• The encoded protein is a serum calcium-decreasing factor that has chymotrypsin-like protease activity. (wikipedia.org)
  • The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. (antikoerper-online.de)
  • In the present work, we further analyzed the peptidase expression in the midgut of sugar-fed females using 1DE-substrate gel zymography, two-dimensional electrophoresis (2DE), mass spectrometry (MS), and protein identification based on similarity. (biomedcentral.com)
  • Our proteomic approach allowed the identification of two different trypsin-like serine peptidases and one chymotrypsin in protein spots of the alkaline region in 2DE map of the A. albopictus female midgut. (biomedcentral.com)
  • These results contribute to the gene annotation in this species of unknown genome and represent a small but important step toward the protein-level functional and localization assignment of trypsin-like serine peptidase genes in the Aedes genus. (biomedcentral.com)
  • The GeNorm tool showed that elongation factor 1α (Elf1a) and ribosomal protein L4 (Rpl4) were the most stable genes, while H3 histone family 3A (Hist3A) and ribosomal protein S18 (RpS18) were the least stable. (bvsalud.org)
  • As in other protein unfoldases of the AAA+ family, the six Rpt subunits in the proteasome base use loops with conserved aromatic residues projecting into the central pore of the hexamer to interact with the substrate polypeptide, mechanically pull on it, and drive its translocation into the 20S core in an ATP hydrolysis-dependent manner. (elifesciences.org)
  • The catalytic activity of the serine proteases from the trypsin family is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which itself is hydrogen-bonded to a serine. (embl.de)
  • A partial list of proteases known to belong to the trypsin family is shown below. (embl.de)
  • It should be noted that bacterial proteases that belong to family S2A are similar enough in the regions of the active site residues that they can be picked up by the same patterns. (embl.de)
  • Zymographic analysis revealed a proteolytic profile composed of at least 13 bands ranging from ~25 to 250 kDa, which were identified as trypsin-like serine peptidases by using specific inhibitors of this class of enzymes. (biomedcentral.com)
  • These results allowed us to detect, identify and characterize the expression of active trypsin-like serine peptidases in the midgut of sugar-fed A. albopictus females. (biomedcentral.com)
  • Serine peptidases are divided into families and subfamilies. (biomedcentral.com)
  • Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. (embl.de)
  • 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)
  • Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. (embl.de)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (embl.de)
  • Cysteine peptidases with an intein-like fold are included in clan PD, which also includes 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)
  • Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. (embl.de)
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (embl.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)
  • Part of the parasite's wide-ranging virulence is attributed to the expression and secretion of large amounts of papain-like cysteine peptidases, namely cathepsin L and cathepsin B [ 3 ]. (biomedcentral.com)
  • The subfamily S1 consists of trypsins, chymotrypsins and elastases, and some serine collagenases were also recently included. (biomedcentral.com)
  • 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)
  • Devel L, Czarny B, Beau F, Georgiadis D, Stura E, Dive V. (2010) Third generation of matrix metalloprotease inhibitors: Gain in selectivity by targeting the depth of the S1' cavity. (guidetoimmunopharmacology.org)
  • Our enzyme kinetics data demonstrates high potency and selectivity of the ppFhCL3 for its cognate FhCL3 enzyme, information that could be utilised to design inhibitors of parasite cathepsin L peptidases. (biomedcentral.com)
  • S1: Chymotrypsin: cathepsin G. Last modified on 10/03/2020. (guidetopharmacology.org)
  • The zoonotic worm parasite Fasciola hepatica secretes an abundance of cathepsin L peptidases that are associated with virulence, invasiveness, feeding and migration. (biomedcentral.com)
  • Little is known, however, about the mechanism by which the propeptide of FhCL3, a cathepsin L peptidase secreted by the infective newly excysted juveniles (NEJs), regulates the inhibition and activation of the mature enzyme before it is secreted into host tissues. (biomedcentral.com)
  • The encoded protease has a specificity similar to that of chymotrypsin C, and may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. (antikoerper-online.de)
  • Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. (icr.ac.uk)
  • Specificity is predominantly directed towards residues that occupy the S1 binding pocket, so that caspases cleave aspartyl bonds, legumains cleave asparaginyl bonds, and gingipains cleave lysyl or arginyl bonds. (embl.de)
  • Chymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: Identity with Rinderknecht's enzyme Y". Proc. (wikipedia.org)
  • This entry represents the active-site-containing domain found in the trypsin family members. (embl.de)
  • the Gla domain , two tandem copies of the EGF domain and a C-terminal trypsin -like peptidase domain which carries out the catalytic cleavage. (wikidoc.org)
  • 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)
  • All the above proteins belong to family S1 in the classification of peptidases [ ( PUBMED:7845208 ) ] and originate from eukaryotic species. (embl.de)
  • In previous studies we characterized the peptidase profile of pre-imaginal stages of A. albopictus and we reported the first proteomic analysis of the midgut from sugar-fed females of this insect species. (biomedcentral.com)
  • the E-value for the Peptidase_C54 domain shown below is 2.3e-39. (embl.de)
  • The peptidases are produced as inactive zymogens that activate at low pH by autocatalytic removal of their N-terminal pro-domain or propeptide. (biomedcentral.com)
  • 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)
  • Infection of the host is dependent on the secretion of a specific set of these peptidases. (biomedcentral.com)
  • Chymotrypsin C is a member of the peptidase S1 family. (wikipedia.org)
  • There are over thirty families in the clan, and tertiary structures have been solved for members of most of these. (embl.de)
  • The family should probably be split up into sub-families. (rcsb.org)
  • Calpains are a family of cytosolic cysteine proteinases. (embl.de)
  • The encoded protein is a serum calcium-decreasing factor that has chymotrypsin-like protease activity. (wikipedia.org)
  • Has chymotrypsin-type protease activity and hypocalcemic activity. (nih.gov)
  • Chymotrypsin C, also known as caldecrin or elastase 4, is an enzyme that in humans is encoded by the CTRC gene. (wikipedia.org)
  • Chymotrypsin B (formerly listed as EC 3.4.4.6), formed from chymotrypsinogen B, is homologous with chymotrypsin A. Enzymes with specificity similar to that of chymotrypsins A and B have been isolated from many species. (enzyme-database.org)