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Serine EndopeptidasesBenzoylarginine NitroanilideCathepsinsEndopeptidasesCathepsin BCathepsin LCathepsin DCathepsin KAmino Acid SequenceNeprilysinMolecular Sequence DataSerineCathepsin GCathepsin HCathepsin ECathepsin CCysteine EndopeptidasesThiorphanCathepsin FProtease InhibitorsPHEX Phosphate Regulating Neutral EndopeptidaseSerine Proteinase InhibitorsCathepsin ZSubstrate SpecificityMetalloendopeptidasesCathepsin WSerine ProteasesDipeptidesLysosomesCystatinsHydrolysisGlycopeptidesCathepsin ACysteine Proteinase InhibitorsKineticsPepstatinsAspartic Acid EndopeptidasesDiazomethaneNeurotensinOligopeptidesLysostaphinHydrogen-Ion ConcentrationEnzyme PrecursorsBase SequencePeptide HydrolasesRecombinant ProteinsPapainPeptide FragmentsElectrophoresis, Polyacrylamide GelSequence Homology, Amino AcidCarboxypeptidasesCloning, MolecularBinding SitesChromatography, High Pressure LiquidPancreatic ElastasePeptidesProtein Processing, Post-TranslationalPhosphorylationIsoflurophateAtrial Natriuretic FactorExopeptidasesMolecular WeightDipeptidyl-Peptidases and Tripeptidyl-PeptidasesThiazepinesCell LineAminopeptidasesEnzyme ActivationLeukocyte ElastaseAmino AcidsCystatin BSerine C-PalmitoyltransferaseSequence AlignmentCysteine ProteasesChromatography, GelCells, CulturedBradykininRNA, MessengerDNA, ComplementaryCystatin AProtein PrecursorsSubstance PThermolysinSubtilisinsCattleMutagenesis, Site-DirectedMutationKidneyLeucineEnkephalin, LeucineFlavobacteriumCarboxypeptidases AHypophosphatemiaBotulinum Toxins, Type AIndansTrypsinChromatography, Ion ExchangeBlotting, WesternProteolysisTrypsin InhibitorsStructure-Activity Relationship

ProteasesTRYPSINPapainProteinProteolyticInhibitorsAspartic acidProteinaseEnzymeCarboxypeptidaseNeutrophilsCatalyticPeptidasesLysosomalProteinasesSpecificityExopeptidasesCleaveResidueRecombinantPeptidesSubtilisinPlasminogenChymotrypsinsSequencesChymaseMetalloproteasesSelectivityEncodesFamilyTissueFoundFunctionsSourceGroup

Proteases22

• In biochemistry , serine proteases or serine endopeptidases (newer name) are a class of peptidases ( enzymes that cleave peptide bonds in proteins ) that are characterised by the presence of a serine residue in the active site of the enzyme . (bionity.com)
• Serine proteases are grouped into clans that share structural homology and then further subgrouped into families that share close sequence homology. (bionity.com)
• Serine proteases participate in a wide range of functions in the body, including blood clotting , immunity , and inflammation , as well as contributing to digestive enzymes in both prokaryotes and eukaryotes. (bionity.com)
• The three serine proteases of the chymotrypsin-like clan that have been studied in greatest detail are chymotrypsin , trypsin , and elastase . (bionity.com)
• Cathepsin C appears to be a central coordinator for activation of many serine proteases in immune/inflammatory cells. (wikipedia.org)
• Once activated by cathepsin C, the proteases are capable of degrading various extracellular matrix components, which can lead to tissue damage and chronic inflammation. (wikipedia.org)
• A cocktail of three protease inhibitors with specificity for the inhibition of metalloproteases, cysteine proteases including cathepsins and papain. (transcriptionfactor.org)
• This cocktail is recommended for inhibition of calcium-dependent endopeptidases, trypsin-like serine proteases, papain, and cysteine proteases. (transcriptionfactor.org)
• Activates serine proteases such as elastase, cathepsin g and granzymes a and b. (lu.se)
• They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation. (lookformedical.com)
• 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)
• Antimicrobial proteins with homology to serine proteases. (uchicago.edu)
• Proteases can be classified into serine proteases, sulfhydryl proteases, metalloproteases and aspartic proteases according to their active centers and optimum pH. (glpbio.com)
• The proteases used in industrial production are mainly endopeptidases. (glpbio.com)
• Acid proteases secreted into the stomach (such as pepsin) and serine proteases present in duodenum (trypsin and chymotrypsin) enable us to digest the protein in food. (stratech.co.uk)
• Other proteases are present in leukocytes (elastase and cathepsin G) and play several different roles in metabolic control. (stratech.co.uk)
• TPP1 encodes a member of the sedolisin family of serine proteases. (novusbio.com)
• Proteases (peptide hydrolases, EC 3.four) are enzymes acting on peptide bonds and include things like the proteinases (endopeptidases, EC 3.four.21-24) along with the exopeptidases (EC 3.two.4.11-19). (rockinhibitor.com)
• These enzymes are expressed as zymogens, which are subsequently processed by other proteolytic enzymes (such as serine proteases, furin, plasmin, and others) to generate the active forms. (periobasics.com)
• Thus the proteases of the pathway - the caspases, cathepsins, and hematopoietic serine proteases - are involved in the normal maintenance of correct cell number, and are therefore implicated in a number of pathologic and physiologic conditions. (salvesenlab.org)
• A group of proteases known as SENPs are involved in both the activation of SUMO precursors (endopeptidase cleavage) and deconjugation of the targets (isopeptidase cleavage). (salvesenlab.org)
• We collaborate extensively with the labs of Marcin Drag and Matt Bogyo to utilize peptide-based substrates and probes to define, visualize, and explore the role of cysteine and serine proteases in cell signaling. (salvesenlab.org)

TRYPSIN1

• Some of them can detach the terminal amino acids from the protein chain (exopeptidases, such as aminopeptidases, carboxypeptidase A), while others attack internal peptide bonds of a protein (endopeptidases, such as trypsin, chymotrypsin, pepsin, papain and elastase). (stratech.co.uk)

Papain3

• Unlike the other members of the papain family, mature cathepsin C consists of four subunits, each composed of the N-terminal proregion fragment, the heavy chain and the light chain. (wikipedia.org)
• these include cathepsin L, papain , and procaricain. (wikipedia.org)
• 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)

Protein8

• The deduced amino acid sequence between the primers was identical to that reported for neutrophil cathepsin G, indicating that the protein of cutaneous mast cells previously shown to be immunologically cross-reactive with neutrophil cathepsin G has a comparable amino acid sequence. (duke.edu)
• Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup of the cysteine cathepsins. (wikipedia.org)
• Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. (wikipedia.org)
• The protein expression levels of PKC delta and PKC epsilon were increased, while cathepsin B, cathepsin S, and cathepsin D were augmented in diabetic db/db kidneys compared to those of wild-type mice. (bvsalud.org)
• 1. Dilute the recombinant mouse Cathepsin B to 10 μg/ml in activation buffer (25 mM MES, 1 mM DTT, pH 5.0) and incubate the protein at 25°C for 3 min. (biolegend.com)
• Endopeptidase cleaves the interior of the protein molecule to form smaller molecular weight peptones and peptones. (glpbio.com)
• The protein is cleaved into a catalytic serine protease chain and a non-catalytic scavenger receptor cysteine-rich chain, which associate via a single disulfide bond. (nih.gov)
• 2008). Trypsins (EC 3.4.21.4) are serine proteinases that will cleave protein chains around the carboxyl side of fundamental Lamino acids. (rockinhibitor.com)

Proteolytic3

• Taken together, these results suggest that high glucose may contribute to an increase in the proteolysis of renal MARCKS, while the upregulation of the cathepsin proteolytic pathway positively correlates with increased proteolysis of MARCKS in diabetic kidneys, where PKC expression is augmented. (bvsalud.org)
• A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. (lookformedical.com)
• Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. (bvsalud.org)

Inhibitors3

• It contains inhibitors of multiple cysteine and serine protease families. (wikipedia.org)
• Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known. (lookformedical.com)
• 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)

Aspartic acid2

• histidine (His 57), serine (Ser 195) (hence the name "serine protease") and aspartic acid (Asp 102). (bionity.com)
• The lysosomal peptidase lysosome family plays an important role in the immune escape process of glioma, which mainly includes aspartic acid cathepsin, serine cathepsin, asparagine endopeptidases, and cysteine cathepsins. (bvsalud.org)

Proteinase3

• This study establishes the primary structure of human skin chymase and provides further evidence for the presence of a cathepsin G-like proteinase within human mast cells. (duke.edu)
• Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils. (uchicago.edu)
• A serine protease which inactivates nucleases Biomolecule/Target: Proteinase K, Recombinant, NGS Grade Alternates names: Protease K, Endopeptidase K, Tritirachium. (telospub.com)

Enzyme6

• The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all serine protease enzymes. (bionity.com)
• The cDNAs encoding rat, human, murine, bovine, dog and two Schistosome cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved. (wikipedia.org)
• The signal peptide is removed during translocation or secretion of the pro-enzyme (pro-cathepsin C) and a large N-terminal proregion fragment (also known as the exclusion domain), which is retained in the mature enzyme, is separated from the catalytic domain by excision of a minor C-terminal part of the pro-region, called the activation peptide. (wikipedia.org)
• Cathepsin C functions as a key enzyme in the activation of granule serine peptidases in inflammatory cells, such as elastase and cathepsin G in neutrophils cells and chymase and tryptase in mast cells. (wikipedia.org)
• 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)
• It is the zymogen form of factor XIIa, an enzyme ( EC 3.4.21.38 ) of the serine protease (or serine endopeptidase) class. (wikidoc.org)

Carboxypeptidase4

• While most cathepsins are exclusively endopeptidases, CTSB exhibits both carboxypeptidase and endopeptidase activities. (biolegend.com)
• Serine-Type D-Ala-D-Ala Carboxypeptidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (rush.edu)
• This graph shows the total number of publications written about "Serine-Type D-Ala-D-Ala Carboxypeptidase" by people in this website by year, and whether "Serine-Type D-Ala-D-Ala Carboxypeptidase" was a major or minor topic of these publications. (rush.edu)
• Below are the most recent publications written about "Serine-Type D-Ala-D-Ala Carboxypeptidase" by people in Profiles. (rush.edu)

Neutrophils2

• UP-cDNA demonstrating amplification products for cathepsin G did not demonstrate amplification products for human neutrophil elastase, suggesting that the cathepsin G PCR amplification product was not derived from neutrophils or monocytes possibly contaminating the lesion. (duke.edu)
• A serine protease found in the azurophil granules of NEUTROPHILS. (lookformedical.com)

Catalytic1

• Subtilisin is evolutionary unrelated to the chymotrypsin-clan, but shares the same catalytic mechanism utilising a catalytic triad , to create a nucleophilic serine . (bionity.com)

Peptidases1

• The zoonotic worm parasite Fasciola hepatica secretes an abundance of cathepsin L peptidases that are associated with virulence, invasiveness, feeding and migration. (biomedcentral.com)

Lysosomal1

• Cathepsin B, also known as CTSB, is a lysosomal cysteine protease. (biolegend.com)

Proteinases1

• These groups include: serine proteinases, cysteine (thiol) proteinases, aspartic proteinases, and matrix metalloproteinases (MMPs). (stratech.co.uk)

Specificity3

• Determination of the crystal structure of Ricistatin in complex with a cysteine cathepsin together with characterization of structural determinants in the Ricistatin binding site explained its restricted specificity. (bvsalud.org)
• A serine endopeptidase that has specificity for cleavage at ARGININE . (nih.gov)
• A CALCIUM-dependent endopeptidase that has specificity for cleavage at ARGININE that is near paired basic residues. (nih.gov)

Exopeptidases2

• Recombinant Ricistatin inhibited host-derived cysteine cathepsins and preferentially targeted endopeptidases, while having only limited impact on proteolysis driven by exopeptidases. (bvsalud.org)
• According to the way they hydrolyze polypeptides, they can be divided into endopeptidases and exopeptidases. (glpbio.com)

Cleave2

• The activity of Cathepsin B is determined by its ability to cleave the fluorogenic peptide substrate, Z-Leu-Arg-AMC (Z=Benzyloxycarbonyl, and AMC=7-amino-4-methylcoumarin) after activation. (biolegend.com)
• The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. (novusbio.com)

Residue1

• Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis. (lookformedical.com)

Recombinant1

• 2. Dilute the recombinant mouse Cathepsin B to 0.05 μg/ml in assay buffer (25 mM MES, pH 5.0). (biolegend.com)

Peptides1

• Antibiotic peptides and serine protease homologs in human polymorphonuclear leukocytes: defensins and azurocidin. (uchicago.edu)

Subtilisin1

• Subtilisin is a serine protease in prokaryotes . (bionity.com)

Plasminogen1

• Activated uPA promotes ECM digestion through serine protease plasminogen. (biolegend.com)

Chymotrypsins1

• Aside from this Chymotrypsins (EC 3.four.21.1), cathepsin B (EC three.four.22.1. (rockinhibitor.com)

Sequences1

• Amplification of the same UP-cDNA with primers coding for the NH2- and COOH-terminal sequences of human neutrophil cathepsin G also produced a specific amplification product which was sequenced. (duke.edu)

Chymase1

• Scholars@Duke publication: Determination of the primary structures of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions. (duke.edu)

Metalloproteases1

• Metzincins are a ubiquitously expressed family of multi-domain zinc (II)-dependent endopeptidases (Stocker and Bode 1995 ), the members of which include well-known metalloproteases such as the matrix metalloproteases (MMPs) (Nagase and Woessner 1999 ), a disintegrin and metalloproteases (ADAMs) (White 2003 ), the ADAMs with a thrombospondin motif (ADAMTS) (Tang 2001 ), the bacterial serralysins (Nakahama et al. (evelinvahter.com)

Selectivity1

• These values are at least 1000-fold lower than those K i obtained for human cathepsin L (HsCL) and human cathepsin K (HsCK) demonstrating the selectivity of the ppFhCL3 for parasite cathepsins L. By exploiting 3-D structural data we identified key molecular interactions in the specific binding between the ppFhCL3 and FhCL3 mature domain. (biomedcentral.com)

Encodes1

• This gene encodes a type II transmembrane serine protease that may be involved in diverse cellular functions, including blood coagulation and the maintenance of cell morphology. (nih.gov)

Family2

• Among them, the cysteine cathepsin family plays a prominent role in the immune escape of glioma. (bvsalud.org)
• This family includes PinA, which inhibits the endopeptidase La. It binds to the La homotetramer but does not interfere with the ATP binding site or the active site of La. (wikipedia.org)

Tissue1

• The primary structure and tissue distribution of cathepsin C". Biological Chemistry Hoppe-Seyler. (wikipedia.org)

Found1

• It is a serine protease ( EC 3.4.21.68 ) found on endothelial cells , the cells that line the blood vessels . (wikidoc.org)

Functions1

• Distinct functions of macrophage-derived and cancer cell-derived cathepsin Z combine to promote tumor malignancy via interactions with the extracellular matrix. (uni-freiburg.de)

Source1

• cathepsin K [Source:HGNC Symbol;Acc. (gsea-msigdb.org)

Group1

• The serine has an -OH group that is able to act as a nucleophile, attacking the carbonyl carbon of the scissile peptide bond of the substrate. (bionity.com)