Cysteine Endopeptidases: ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.Cathepsin B: A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Neprilysin: Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Cathepsins: A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.Cathepsin L: A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.Cystatins: A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.Papain: A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Thiorphan: A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.Peptide Hydrolases: Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.Calpain: Cysteine proteinase found in many tissues. Hydrolyzes a variety of endogenous proteins including NEUROPEPTIDES; CYTOSKELETAL PROTEINS; proteins from SMOOTH MUSCLE; CARDIAC MUSCLE; liver; platelets; and erythrocytes. Two subclasses having high and low calcium sensitivity are known. Removes Z-discs and M-lines from myofibrils. Activates phosphorylase kinase and cyclic nucleotide-independent protein kinase. This enzyme was formerly listed as EC 3.4.22.4.HIV Protease: Enzyme of the human immunodeficiency virus that is required for post-translational cleavage of gag and gag-pol precursor polyproteins into functional products needed for viral assembly. HIV protease is an aspartic protease encoded by the amino terminus of the pol gene.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Cysteine Dioxygenase: An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.Kinetics: The rate dynamics in chemical or physical systems.PHEX Phosphate Regulating Neutral Endopeptidase: A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Dipeptides: Peptides composed of two amino acid units.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.Cysteine Synthase: An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.Cathepsin K: A cysteine protease that is highly expressed in OSTEOCLASTS and plays an essential role in BONE RESORPTION as a potent EXTRACELLULAR MATRIX-degrading enzyme.Cathepsin F: A lysosomal papain-related cysteine proteinase that is expressed in a broad variety of cell types.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Caspases: A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.Oligopeptides: Peptides composed of between two and twelve amino acids.Sulfhydryl Compounds: Compounds containing the -SH radical.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Cell Line: Established cell cultures that have the potential to propagate indefinitely.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Bacterial Proteins: Proteins found in any species of bacterium.Molecular Weight: The sum of the weight of all the atoms in a molecule.Caspase 1: A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Proteolysis: Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.Cathepsin C: A papain-like cysteine protease that has specificity for amino terminal dipeptides. The enzyme plays a role in the activation of several pro-inflammatory serine proteases by removal of their aminoterminal inhibitory dipeptides. Genetic mutations that cause loss of cathepsin C activity in humans are associated with PAPILLON-LEFEVRE DISEASE.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Spirometra: A genus of tapeworms of the family Diphyllobothriidae, which are parasites of fish-eating cats, dogs, and birds. Infection in man is caused by eating undercooked fish. The larval form is called SPARGANUM.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Protease La: A prokaryotic ATP-dependent protease that plays a role in the degradation of many abnormal proteins. It is a tetramer of 87-kDa subunits, each of which contains a proteolytic site and a ATP-binding site.Apoptosis: One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.Protein PrecursorsLeucine: An essential branched-chain amino acid important for hemoglobin formation.Caspase 3: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Cystine: A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)DNA Cleavage: A reaction that severs one of the covalent sugar-phosphate linkages between NUCLEOTIDES that compose the sugar phosphate backbone of DNA. It is catalyzed enzymatically, chemically or by radiation. Cleavage may be exonucleolytic - removing the end nucleotide, or endonucleolytic - splitting the strand in two.Glycopeptides: Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.ATP-Dependent Proteases: Proteases that contain proteolytic core domains and ATPase-containing regulatory domains. They are usually comprised of large multi-subunit assemblies. The domains can occur within a single peptide chain or on distinct subunits.Streptococcus pyogenes: A species of gram-positive, coccoid bacteria isolated from skin lesions, blood, inflammatory exudates, and the upper respiratory tract of humans. It is a group A hemolytic Streptococcus that can cause SCARLET FEVER and RHEUMATIC FEVER.Paragonimus: A genus of lung flukes of the family Troglotrematidae infecting humans and animals. This genus consists of several species one of which is PARAGONIMUS WESTERMANI, a common lung fluke in humans.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Cystatin B: An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Coumarins: Synthetic or naturally occurring substances related to coumarin, the delta-lactone of coumarinic acid.Bromelains: Protein-digesting and milk-clotting enzymes found in PINEAPPLE fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. This enzyme was formerly listed as EC 3.4.22.4.Helminth Proteins: Proteins found in any species of helminth.Cystatin A: A cytastin subtype found at high levels in the SKIN and in BLOOD CELLS. Cystatin A incorporates into the cornified cell envelope of stratified squamous epithelial cells and may play a role in bacteriostatic properties of skin.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Caspase 6: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 7; CASPASE 8; and CASPASE 10. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Amino Acid Chloromethyl Ketones: Inhibitors of SERINE ENDOPEPTIDASES and sulfhydryl group-containing enzymes. They act as alkylating agents and are known to interfere in the translation process.Protozoan Proteins: Proteins found in any species of protozoan.Leupeptins: A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Chromatography, Gel: Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Mass Spectrometry: An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.DiazomethanePlant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Sulfhydryl Reagents: Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.Cathepsin W: A cysteine endopeptidase found in NATURAL KILLER CELLS and CYTOTOXIC T-LYMPHOCYTES. It may have a specific function in the mechanism or regulation of cytolytic activity of immune cells.Neurotensin: A biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.Protease Nexins: Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.Cystatin C: An extracellular cystatin subtype that is abundantly expressed in bodily fluids. It may play a role in the inhibition of interstitial CYSTEINE PROTEASES.Chromatography, Ion Exchange: Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Exopeptidases: A sub-class of PEPTIDE HYDROLASES that act only near the ends of polypeptide chains.Serpins: 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. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. 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.Chymotrypsin: A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side.Dithiothreitol: A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.Lysostaphin: A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC 3.4.24.75.Iodoacetamide: An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Ubiquitin-Specific Proteases: Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Cleavage Stage, Ovum: The earliest developmental stage of a fertilized ovum (ZYGOTE) during which there are several mitotic divisions within the ZONA PELLUCIDA. Each cleavage or segmentation yields two BLASTOMERES of about half size of the parent cell. This cleavage stage generally covers the period up to 16-cell MORULA.Pepstatins: N-acylated oligopeptides isolated from culture filtrates of Actinomycetes, which act specifically to inhibit acid proteases such as pepsin and renin.Metalloproteases: Proteases which use a metal, normally ZINC, in the catalytic mechanism. This group of enzymes is inactivated by metal CHELATORS.Glutathione: A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Time Factors: Elements of limited time intervals, contributing to particular results or situations.Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Thermolysin: A thermostable extracellular metalloendopeptidase containing four calcium ions. (Enzyme Nomenclature, 1992) 3.4.24.27.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
Reaction mechanism of the cysteine protease mediated cleavage of a peptide bond. ... Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... In fact, dozens of latices of different plant families are known to contain cysteine proteases.[1] Cysteine proteases are used ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ...
It also mediates cleavage of clumping factor B causing loss of binding of S. aureus to fibrinogen. By this it may act as a self ... a cysteine protease. Aureolysin cleaves different proteins among inflammatory regulators and immune components. Aureolysin can ... it proteolytically activates the zymogen of the serine protease glutamyl endopeptidase, which in turn is the activator of ... The cleavage of α1-antitrypsin generates a fragment chemotactic to neutrophils. Aureolysin has also been shown to cleave the ...
... , also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and ... including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. ... Amino acid residues within the pro-region mediate their membrane association, and play a role in the transport of the proenzyme ... The proteins are typically lysosomal or secreted, and proteolytic cleavage of the propeptide is required for enzyme activation ...
In humans, the group of cathepsin cysteine proteases or cysteine cathepsins comprises 11 family members, cathepsins B, C, F, H ... The propeptide is removed through cleavage by a furin type protease yielding the active enzyme. The propeptide of most MMPs is ... These effects are mediated by interacting and interfering with various angiogenic related proteins such as integrins and serine ... MMPs are a large multigene family of zinc-dependent endopeptidases. The collective MMP family is capable of degrading all known ...
... a cysteine protease with the proregion covalently linked to the active site cysteine". Journal of Molecular Biology. 295 (4): ... It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin Z has an ... "RGD-dependent binding of procathepsin X to integrin alphavbeta3 mediates cell-adhesive properties". The Journal of Biological ... "Maturation of dendritic cells depends on proteolytic cleavage by cathepsin X". Journal of Leukocyte Biology. 84 (5): 1306-15. ...
Cathepsin K is a collagenolytic, papain-like, cysteine protease that is mainly expressed in osteoclasts, and is secreted into ... It is synthesized as a proenzyme with a molecular weight of 37kDa, and upon activation by autocatalytic cleavage, is ... The positioning of this "sealing zone" appears to be mediated by integrins expressed on the osteoclast surface. With the ... The matrix metalloproteinases (MMPs) comprise a family of more than 20 zinc-dependent endopeptidases. The role of matrix ...
... are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ... Protease 3C and 2A are also responsible for the cleavage of translation initiation eIF4GE and poly-A- binding protein, PABP. ... Protease 2A and 3C also induce apoptosis via intrinsic mitochondria mediated apoptosis, which leads to the release of ... Picornain 3C (EC 3.4.22.28, Picornain 3C is a protease and endopeptidase enzyme found in the picornavirus, that cleaves peptide ...
The disintigrin and cysteine-rich domain (shown to the right) plays an essential role in regulation of protease activity in ... 2003). "ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles". FASEB J. 17 (2 ... "Entry of ADAM10 endopeptidase (EC-Number 3.4.24.81 )". Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E ... Hattori M, Osterfield M, Flanagan JG (2000). "Regulated cleavage of a contact-mediated axon repellent". Science. 289 (5483): ...
Serine proteases - using a serine alcohol Cysteine proteases - using a cysteine thiol Threonine proteases - using a threonine ... For example, TEV protease is specific for the sequence ...ENLYFQ\S... ('\'=cleavage site). Proteases, being themselves proteins ... "Senescence-dependent degradation of Lhcb3 is mediated by a thylakoid membrane-bound protease". Journal of plant physiology. 161 ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). Catalysis is achieved by one of two mechanisms: ...
Serine protease. *Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome ... For example, TEV protease is specific for the sequence ...ENLYFQ\S... ('\'=cleavage site).[7] ... "Senescence-dependent degradation of Lhcb3 is mediated by a thylakoid membrane-bound protease". Journal of Plant Physiology. 161 ... The activity of proteases is inhibited by protease inhibitors.[18] One example of protease inhibitors is the serpin superfamily ...
Glutamyl endopeptidase proteolytically activates the zymogen of the cysteine protease staphopain B (staphopain A is activated ... It has been suggested, however, that the protease promotes S. aureus dissemination through cleavage of self-proteins and ... "Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus". The Journal of Biological Chemistry. ... Glutamyl endopeptidase (EC 3.4.21.19, SspA, V8 protease, GluV8, endoproteinase Glu-C, staphylococcal serine proteinase) is an ...
The known autolytic cleavage is mediated by the nodavirus endopeptidase, from the C-terminus of the coat protein and only ... Asparagine Lyase Protein precursor Proteolysis Nucleophilic substitution Protease cysteine- serine- threonine- aspartic- ... The existence of this seventh catalytic type of proteases, in which the peptide bond cleavage occurs by self-processing instead ... Family N2: Includes tetraviruses endopeptidases. The known autolytic cleavage is from the C-terminus of the coat protein. The ...
The dissociation of cysteine -Zinc coordination starts from the cleavage of the first 30 amino acids of the prodomain, which ... The expression of MMP7 is regulated by the Wnt/ β catenin signaling pathway, and mediated by transformation growth factor β ( ... Matrilysin also known as matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an ... MMP7 is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. ...
Wilk S, Orlowski M (March 1983). "Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease ... Apoptosis is mediated through disrupting the regulated degradation of pro-growth cell cycle proteins.[88] However, some cell ... This is then transferred to E1's active-site cysteine residue in concert with the adenylylation of a second ubiquitin.[48] This ... "Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants". The Journal of ...
protease binding. • protein self-association. • peptidase activity. • protein binding. • kinase activator activity. • cysteine- ... Since A20 has been described has an inhibitor of NF-κB, this suggests that paracaspase-mediated A20 cleavage in T lymphocytes ... type endopeptidase activity. • hydrolase activity. • identical protein binding. Cellular component. • cytoplasm. • plasma ... "T cell antigen receptor stimulation induces MALT1 paracaspase-mediated cleavage of the NF-kappaB inhibitor A20". Nature ...
positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • negative regulation of ... necrosis-like programmed cell death mediated by serine protease activity". Blood. 103 (6): 2299-307. doi:10.1182/blood-2003-05- ... "Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in ... positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • protein homotrimerization. ...
Pro-inflammatory and pro-angiogenic responses are activated by TF/VIIa mediated cleavage by the protease-activated receptor 2 ( ... activation of cysteine-type endopeptidase activity involved in apoptotic process. • positive regulation of positive chemotaxis ... serine-type endopeptidase activity. • protease binding. Cellular component. • membrane. • extracellular matrix. • intrinsic ... The complex of TF with factor VIIa catalyzes the conversion of the inactive protease factor X into the active protease factor ...
This process is mediated by a specialized enzyme called DHHC palmitoyl transferase. The cysteine rich domain of SNAP-25 has ... This cleavage of synaptobrevin is the final target of TeNT and even in low doses the neurotoxin will inhibit neurotransmitter ... The light chain has zinc-dependent endopeptidase or more specifically matrix metalloproteinase (MMP) activity through which ... "Tetanus toxin is a zinc protein and its inhibition of neurotransmitter release and protease activity depend on zinc". The EMBO ...
activation of cysteine-type endopeptidase activity involved in apoptotic process. • tumor necrosis factor-mediated signaling ... Nevertheless, TRADD binds FADD, which then recruits the cysteine protease caspase-8. A high concentration of caspase-8 induces ... is released via proteolytic cleavage by the metalloprotease TNF alpha converting enzyme (TACE, also called ADAM17).[26] The ... positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • negative regulation of viral ...
... cleavage is mediated by the calpain family of calcium-dependent cytosolic proteases. ... positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • branching involved in ureteric bud ... Upon cleavage, the C-terminus of Myc (containing the DNA binding domain) is degraded, while Myc-nick, the N-terminal segment ... Myc-nick is a cytoplasmic form of Myc produced by a partial proteolytic cleavage of full-length c-Myc and N-Myc.[15] ...
... prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer peptide ... T-helper cell mediated) response. One protease-resistant peptide from α-gliadin contains a region that stimulates lymphocytes ... Deamidation is the reaction by which a glutamate residue is formed by cleavage of the epsilon-amino group of a glutamine side ... The inflammatory process, mediated by T cells, leads to disruption of the structure and function of the small bowel's mucosal ...
serine-type endopeptidase activity. • cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. ... Dunn AD, Crutchfield HE, Dunn JT (October 1991). "Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by ... regulates ABCA1-mediated lipid efflux". The Journal of Biological Chemistry. 281 (52): 39971-81. doi:10.1074/jbc.M605095200. ... Cathepsin D is a protein that in humans is encoded by the CTSD gene.[5][6] This gene encodes a lysosomal aspartyl protease ...
Proteasome activator complex subunit 3 is a protein that in humans is encoded by the PSME3 gene. The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S ...
... s, also known as thiol proteases, are enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers. The MEROPS protease classification system counts 14 superfamilies plus several currently unassigned families (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold ...
26S proteasome non-ATPase regulatory subunit 13 is an enzyme that in humans is encoded by the PSMD13 gene. The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. Two transcripts encoding different isoforms have been described. The Proteasome and its subunits are of ...
... , also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). Papain belongs to a family of related proteins with a wide variety of activities, including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. Members of the papain family are widespread, found in baculoviruses, eubacteria, yeast, and practically all protozoa, plants and mammals. The proteins are typically lysosomal or secreted, and proteolytic cleavage of the propeptide is required for enzyme activation, although bleomycin hydrolase is cytosolic in fungi and mammals. Papain-like cysteine proteinases are essentially synthesised as inactive proenzymes (zymogens) with N-terminal propeptide regions. The activation process of these enzymes includes the removal of ...
... is a protein that in humans is encoded by the CTSF gene. Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. In general, cathepsins contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be ...
26S proteasome non-ATPase regulatory subunit 14, also known as 26S proteasome non-ATPase subunit Rpn11, is an enzyme that in humans is encoded by the PSMD14 gene. This protein is one of the 19 essential subunits of a complete assembled 19S proteasome complex. Nine subunits Rpn3, Rpn5, Rpn6, Rpn7, Rpn8, Rpn9, Rpn11, SEM1(Yeast analogue for human protein DSS1), and Rpn12 form the lid sub complex of 19S regulatory particle for proteasome complex. The gene PSMD14 encodes one of 26S proteasome non-ATPase subunit. The human gene PSMD14 has 12 Exons and locates at chromosome band 2q24.2. The human protein 26S proteasome non-ATPase regulatory subunit 14 is 34.6 kDa in size and composed of 310 amino acids. The calculated theoretical pI of this protein is 6.06. 26S proteasome complex is usually consisted of a 20S core particle (CP, or 20S proteasome) and one or two 19S regulatory particles (RP, or 19S proteasome) on either one side or both side of the barrel-shaped 20S. The CP and RPs pertain distinct ...
26S proteasome non-ATPase regulatory subunit 1, also as known as 26S Proteasome Regulatory Subunit Rpn2 (systematic nomenclature), is a protein that in humans is encoded by the PSMD1 gene. This protein is one of the 19 essential subunits that contributes to the complete assembly of 19S proteasome complex. The gene PSMD1 encodes the largest non-ATPase subunit of the 19S regulator base, which is responsible for substrate recognition and binding. The human PSMD1 gene has 25 exons and locates at chromosome band 2q37.1. The human protein 26S proteasome non-ATPase regulatory subunit 1 is 106 kDa in size and composed of 953 amino acids. The calculated theoretical pI of this protein is 5.25. An alternative splicing during gene expression generates an isoform of the protein in which the amino acid sequence from 797-827 is missing. 26S proteasome complex is usually consisted of a 20S core particle (CP, or 20S proteasome) and one or two 19S regulatory particles (RP, or 19S proteasome) on either one side or ...
Proteasome subunit alpha type-3 also known as macropain subunit C8 and proteasome component C8 is a protein that in humans is encoded by the PSMA3 gene. This protein is one of the 17 essential subunits (alpha subunits 1-7, constitutive beta subunits 1-7, and inducible subunits including beta1i, beta2i, beta5i) that contributes to the complete assembly of 20S proteasome complex. The eukaryotic proteasome recognized degradable proteins, including damaged proteins for protein quality control purpose or key regulatory protein components for dynamic biological processes. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. As a component of alpha ring, proteasome subunit alpha type-3 contributes to the formation of heptameric alpha rings and substrate entrance gate. The human protein proteasome subunit alpha type-3 is 28.4 kDa in size and composed of 254 amino acids. The calculated theoretical pI of this protein is 5.08. The proteasome is a ...
Proteasome subunit beta type-10 as known as 20S proteasome subunit beta-2i is a protein that in humans is encoded by the PSMB10 gene. This protein has a major role in the immune system as part of an immunoproteasome that is primarily induced upon infection and formed by replacing constitutive beta subunits with inducible beta subunits which possess specific cleavage properties that aid in the release of peptides necessary for MHC class I antigen presentation. The immunoproteasome appears to have a pivotal role in modulating NFκB signaling. This gene PSMB10 encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. Proteolytic processing is required to generate a mature subunit. Expression of this gene is induced by gamma interferon, and this gene product replaces catalytic subunit beta2 (proteasome subunit beta type-7) in the immunoproteasome. The human PSMB10 gene has 8 exons and locates at chromosome band 16q22.1. The human protein ...
... s (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death (including apoptosis, pyroptosis and necroptosis) and inflammation. They are named caspases due to their specific cysteine protease activity - a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 11 or 12 confirmed caspases in humans[note 1] and 10 in mice, carrying out a variety of cellular functions. The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during ...
... s (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death (including apoptosis, pyroptosis and necroptosis) and inflammation. They are named caspases due to their specific cysteine protease activity - a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 11 or 12 confirmed caspases in humans[note 1] and 10 in mice, carrying out a variety of cellular functions.. The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during ...
... is a protein that in humans is encoded by the CTSW gene.[5][6][7]. The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2.[7]. ...
Martin, S.J., Amarante-Mendes, G.P., Shi, L., Chuang, T.H., Casiano, C.A., O'Brien, G.A., Fitzgerald, P., Tan, E.M., Bokoch, G.M., Greenberg, A.H. and Green, D.R. (1996). „The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease, CPP32, via a novel two-step mechanism". EMBO J. 15: 2407-2416. PMID 8665848 ...
IgdE is the founding member of a novel cysteine protease family (C113). Novel streptococcal members of this protease family ... Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to ... Streptococcus pyogenes, Group A Streptococci, GAS, virulence factor, IdeS, SpeB, cysteine protease, protease inhibitor, IgG, ... Open this publication in new window or tab ,,Studies on secreted cysteine proteases of Streptococcus pyogenes: IdeS and SpeB. ...
IgdE is the founding member of a novel cysteine protease family (C113). Novel streptococcal members of this protease family ... Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to ... Streptococcus pyogenes, Group A Streptococci, GAS, virulence factor, IdeS, SpeB, cysteine protease, protease inhibitor, IgG, ... 1. Studies on secreted cysteine proteases of Streptococcus pyogenes: IdeS and SpeB. Öppna denna publikation i ny flik eller ...
Using AEP-mediated cleavage sequences, we modeled the effects of the protease on ASNase and created a number of recombinant ... Asparaginyl endopeptidase (AEP), which is overexpressed predominantly in high-risk subsets of ALL, specifically degraded ASNase ... Here, we now report that 2 lysosomal cysteine proteases present in lymphoblasts are able to degrade l-asparaginase. Cathepsin B ... A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug l. -asparaginase ...
Reaction mechanism of the cysteine protease mediated cleavage of a peptide bond. ... Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... In fact, dozens of latices of different plant families are known to contain cysteine proteases.[1] Cysteine proteases are used ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ...
Enzymatic characterization of the streptococcal endopeptidase, IdeS, reveals that it is a cysteine protease with strict ... Antibody-mediated rejection occurred in 10 patients (7 patients in the U.S. study and 3 in the Swedish study) at 2 weeks to 5 ... Therapeutic cleavage of IgG: new avenues for treating inflammation. Nandakumar et al. TRENDS IN IMMUNOLOGY, Vol. 29, Issue 4, ... Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. Wenig et al. PNAS Dec ...
... cleavage at the AAX tripeptide and methylation of the carboxyl-prenylated cysteine residue. The major CAAX protease activity is ... mediated by Rce1 (Ras and a-factor converting enzyme 1), an intramembrane protease (IMP) of the endoplasmic reticulum. ... Here we report the crystal structure of a Methanococcus maripaludis homologue of Rce1, whose endopeptidase specificity for ... where C is cysteine, A is an aliphatic amino acid and X is any amino acid). These reactions involve prenylation of the cysteine ...
It also mediates cleavage of clumping factor B causing loss of binding of S. aureus to fibrinogen. By this it may act as a self ... a cysteine protease. Aureolysin cleaves different proteins among inflammatory regulators and immune components. Aureolysin can ... it proteolytically activates the zymogen of the serine protease glutamyl endopeptidase, which in turn is the activator of ... The cleavage of α1-antitrypsin generates a fragment chemotactic to neutrophils. Aureolysin has also been shown to cleave the ...
This led to the idea that the introduction by AEP of a very limited number of cleavages mediated an essential unlocking step, ... Asparaginyl endopeptidase: case history of a class II MHC compartment protease. Immunol. Rev. 207: 218-228. ... Other cysteine proteases can initiate TTCF processing. We obtained more efficient TTCF digestion by wild-type DCs when we ... However, this cleavage was also detected when AEP-null lysosomes were used, suggesting that other lysosomal proteases could ...
Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and ... including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endo-peptidase activity. ... Amino acid residues within the pro-region mediate their membrane association, and play a role in the transport of the proenzyme ... The proteins are typically lysosomal or secreted, and proteolytic cleavage of the propeptide is required for enzyme activation ...
Cysteine endopeptidase assay.Cysteine protease activity present in ammonium sulfate-precipitated culture supernatants was ... Tn917-mediated transposon mutagenesis.The Tn917-mediated transposon mutagenesis was performed as previously described (21, 28 ... The cleavage of substrate and generation of product were determined to be linear with time to an A405 of 1.5. The cysteine ... In addition, analysis of β-hemolysis, streptokinase production, and secretion of a cysteine protease were included in the ...
aspartic-type endopeptidase activity; cysteine-type endopeptidase activity; cysteine-type endopeptidase activity; cysteine-type ... Activation of caspases through apoptosome-mediated cleavage, organism-specific biosystem; Alzheimers disease, organism-specific ... apoptotic protease MCH-3; ICE-like apoptotic protease 3; caspase 7, apoptosis-related cysteine protease; CMH-1; ICE-LAP3;. ... CASP7; caspase 7, apoptosis-related cysteine peptidase; caspase 7, apoptosis related cysteine protease; caspase-7; CMH 1; ICE ...
Activation of the pro-protease likely occurs by furin-mediated cleavage of the pro-domain at the N-terminus and further C- ... These secreted proteases share similar functional domains including a pro-protease metalloproteinase disintegrin-like cysteine- ... collagen processing blood coagulation cell migration and arthritis and several family members are glutamyl-endopeptidases that ... These changes are mediated by the cytokines released from infiltrating inflammatory cells and enterocytes in paracrine or ...
Activation of the pro-protease likely occurs by furin-mediated cleavage of the pro-domain at the N-terminus and further C- ... These secreted proteases share similar functional domains including a pro-protease metalloproteinase disintegrin-like cysteine- ... collagen processing blood coagulation cell migration and arthritis and several family members are glutamyl-endopeptidases that ... Increased expression and activation of endogenous proteases that cleave the PG core would be one mechanism to enhance neural ...
Cysteine protease CPP32; PARP cleavage protease; SREBP cleavage activity 1; Yama protein; SREBP cleavage activity 1; caspase 3 ... CSN-mediated deneddylation is regulated by active CASP3. CASP-3 cleavage of RAD51 results in a functional decrease in RAD51 ... cyclin-dependent protein kinase inhibitor activity; cysteine-type endopeptidase activity; peptidase activity; protein binding. ... CASP3 is part of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspase-3 enzyme results in the ...
One study showed that TLR9 proteolysis is a multistep process with the initial cleavage that can be mediated by AEP or multiple ... TLR7 and TLR9 are cleaved within their ectodomains by pH-sensitive cysteine endopeptidases. Cathepsins (CTS) B, K, L, and S, ... several groups have reported somewhat controversial results on the role of specific proteases (Matsumoto F et al 2008, Park B ... TLR7 and TLR3 were reported to be cleaved in a similar manner (Ewald SE et al 2011). Cleavage of TLR3 is not shown in this ...
Schmid M, Simpson D, Kalousek F, Gietl C (1998) A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean ... correct cleavage site can be achieved also by other unrelated proteases such as the ricinosome-localized KDEL-tailed cysteine ... 2005). Regulation of proteases through CaM is not widespread, but there are other examples such as the Ca2+-dependent cysteine ... Recombinant AtDEG15 exhibits the characteristics of the monomer as a general protease with an intrinsic self-cleavage activity ...
NPM1 cleavage is abrogated on LPS-mediated activation. LPS is a macrophage activator through TLR4. Exposure of M-CSF-induced ... Proteolysis of cellular components by cysteine proteases, including various combinations of caspases and cathepsins, has been ... because the endopeptidase activity of some cathepsins could be conserved at neutral pH.30 The 20-kDa N-terminal fragment of ... The cytotoxic granule protease granzyme M cleaves NPM1 at Leu-158 during natural killer cell-mediated killing, which was ...
Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis ... This enzyme is necessary for target cell lysis in cell-mediated immune responses. It cleaves after Asp. Seems to be linked to ... Preferential cleavage: -Asp- -Xaa- ,, -Asn- -Xaa- , -Met- -Xaa-, -Ser- -Xaa-. *GRAB_HUMAN,P10144 ... GO annotations related to this gene include serine-type endopeptidase activity and serine-type peptidase activity. An important ...
Cysteine Proteinase Inhibitors,Cytochrome c Group,Cytoplasm,Endopeptidases,Enzyme Activation,Enzyme Precursors,Extracellular ... A broad-range caspase inhibitor, zVAD-fmk, blocked the caspase activation, the cleavage of proteins, and DNA fragmentation, ... we conclude that this process does not involve the CD95-mediated pathway. While MAL did not directly activate caspases in the ... Protease activation in apoptosis induced by MAL. Köhler, C; Håkansson, Anders P LU ; Svanborg, C LU ; Orrenius, S and ...
2013) Rapid IgG heavy chain cleavage by the streptococcal IgG endopeptidase IdeS is mediated by IdeS monomers and is not due to ... a cysteine protease that specifically cleaves all four subclasses of human IgG in the lower hinge region of the heavy chain, ... 2010) Cleavage of IgGs by proteases associated with invasive diseases: an evasion tactic against host immunity? MAbs 2, 212-220 ... S. pyogenes produces IdeS, a protease cleaving IgG in the lower hinge region and we find highly effective IdeS-cleavage of IgG ...
... and the lysosomal protease Asparagine endopeptidase (AEP) [61, 77] are also cysteine proteases that are present in ... Zhang Z et al (2014) Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimers disease ... These dipeptidases are cysteine-dependent peptidases that specifically hydrolyze X-Pro motifs [63]. A large number of proteases ... Ferreira A, Bigio EH (2011) Calpain-mediated tau cleavage: a mechanism leading to neurodegeneration shared by multiple ...
Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimers disease. Nat Med. 2014 Nov;20 ... Knocking out this cysteine protease partially rescued both tau pathology and behavioral deficits in transgenic mice expressing ... Paper: Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimers disease. ... Cleavage of tau] is another means by which the asparaginyl endopeptidase could promote tau pathology." Like the authors, he ...
Hook, V. et al., "`Prohormone Thiol Protease` (PTP), a novel Cysteine Protease for Proenkephalin and Prohormone Processing," In ... Like the .beta.-secretase and the .gamma.-secretase, the protease responsible for that cleavage has also not been isolated but ... Meckelein, B. et al., "Human Endopeptidase (THOP1) Is Localized on Chromosome 19 Within the Linkage Region for the Late-Onset ... Amyloid Precursor Protein and Mediates Its Degradation," Cell., 82:331-340 (1995)... Kreiger, T. et al., "Purification and ...
... an endopeptidase-like cleavage followed by carboxypeptidase-like processive cleavage. Utilizing small molecule inhibitors/ ... RIP proteases mediate various key life events by releasing bioactive peptides from the plane of the membrane region. We have ... Using a substituted cysteine accessibility method, we have previously shown that the hydrophilic "catalytic pore" structure of ... Although γ-secretase is a responsible protease to generate Aβ through a processive cleavage, the proteolytic mechanism of γ- ...
This attachment induces virion internalization predominantly through clathrin-mediated endocytosis. ... Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its ... Selective cleavage of Tyr-,-Gly bond in the picornavirus polyprotein.. Selective cleavage of Gln-,-Gly bond in the poliovirus ... Clathrin-mediated endocytosis of virus by host, Host-virus interaction, Ion transport, Transport, Viral attachment to host cell ...
  • However, many neo-N-, or C-terminal peptides protease trypsin has become the dominant workhorse for the are too short for mass spectrometry-based identification when proteome digestions due to its high cleavage efficiency, high only a single protease is used. (deepdyve.com)
  • Digestion of prolamins with barley endoprotease B2 (EP-HvB2) combined with Flavobacterium meningosepticum prolyl endopeptidase (PE-FmPep) or Pyrococcus furiosus prolyl endopeptidase (PE-PfuPep) significantly reduced (up to 67%) the amount of the indigestible gluten peptides of all prolamin families tested. (springer.com)
  • Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use. (abcam.com)
  • As a result of its exceptional structure, proline determines in such peptides both their conformation and stability, preventing degradation by non-specific proteases. (justia.com)
  • These peptides are produced mainly from antigens that have been internalized and processed in the endocytic pathway of APCs, where they meet class II molecules en route to the cell surface ( 1 , 2 ). (rupress.org)
  • Different types of APC (like DC, B lymphoblastoid cells (BLC), thymic epithelial cells, monocytes) express individual patterns of active endocytic proteases and little is known about the rules that govern proteolysis of Ag in human DC. (jimmunol.org)
  • MMP-7 proteolysis generated four major fragments (26 kDa, 17 kDa, 15.5 kDa, and 15.5 kDa), and two cleavage sites were identified: one at the site of hydrolysis of the K 144 -I 145 peptide bond and one at the R 95 -L 96 peptide bond. (aacrjournals.org)
  • Proteases play a fundamental and essential role in many biological and pathological processes by the regulatory mechanism, proteolysis. (thno.org)
  • Pathogen-mediated proteolysis of the cell death regulator RIPK1 and the host defense modulator RIPK2 in human aortic endothelial cells. (nih.gov)
  • To determine if P. gingivalis-induced proteolysis of RIPK2 was a result of cell activation via TLR or NLR-mediated signaling, HAEC were treated with a panel of synthetic or purified agonists to PRR that have been demonstrated to be activated by P. gingivalis or are direct activators of the NOD/RIPK2 signaling pathway. (nih.gov)
  • Aureolysin (EC 3.4.24.29, protease III, staphylococcal metalloprotease, Staphylococcus aureus neutral proteinase) is an extracellular metalloprotease expressed by Staphylococcus aureus. (wikipedia.org)
  • Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). (wikipedia.org)
  • Trypsin, which cuts specifically after the basic residues lysine and arginine, is the predominant enzyme used for proteome digestion, although proteases with alternative specificities are required to detect sequences that are not accessible after tryptic digest. (deepdyve.com)
  • Taken together, we demonstrate that legumain is a practical, efficient protease for extending the proteome and sequence coverage achieved with trypsin, with unique possibilities for the characterization of post-translational modification sites. (deepdyve.com)
  • Each family may contain many hundreds of related proteases (e.g. trypsin , elastase , thrombin and streptogrisin within the S1 family). (wikipedia.org)
  • Examples of these folds are observed in trypsin, subtilisin, prolyl oligopeptidase, and ClpP protease. (schoolbag.info)
  • 3. The method according claim 1, wherein the labile peptide linker is labile to one or more proteases present in the intestinal tract such that greater than 50% by mass of the construct is cleaved into first and second immunoglobulin chain variable domains after 160 minutes after mixing in the Trypsin Protease Assay. (patents.com)
  • 7. The method according to claim 1, wherein the labile peptide linker comprises a cleavage site for trypsin or a trypsin-like protease. (patents.com)
  • The PA clan of endopeptidases is the most abundant and over two thirds of this clan is comprised of the S1 family of serine proteases, which bear the archetypal trypsin fold and have a catalytic triad in the order Histidine, Aspartate, Serine. (pubmedcentralcanada.ca)
  • Asparagine endopeptidase (AEP) or legumain is a potentially important Ag-processing enzyme that introduces limited cleavages that trigger unfolding and class II MHC binding of different Ag substrates. (jimmunol.org)
  • 1999 The conversation of the Canertinib ADAMTS domains with their substrates is usually complex and may involve binding via the thrombospondin type 1 motif and/or sequences in the C-terminal spacer or cysteine-rich region of the molecule (Flannery et al. (technumber.com)
  • Intramembrane proteases have the unusual property of cleaving their substrates in the plane of cellular membranes. (biologists.org)
  • Streptococcus pyogenes employs an IgG specific endopeptidase, IdeS, to counteract the effector functions of specific IgG. (diva-portal.org)
  • The IgG-degrading enzyme derived from Streptococcus pyogenes(IdeS), an endopeptidase, cleaves human IgG into F(ab′)2 and Fc fragments inhibiting complement-dependent cytotoxicity and antibody-dependent cellular cytotoxicity, which suggests that IdeS might be useful for desensitization. (hansamedical.com)
  • Here we applied a combined mass spectrometry-based proteomics strategy to investigate how the human proteome is transiently modified by the pathogen Streptococcus pyogenes , with a particular focus on bacterial cleavage of IgG in vivo . (mcponline.org)
  • Group A Streptococcus (GAS) acquires mutations of the virulence regulator CovRS in human and mouse infections, and these mutations result in the upregulation of virulence genes and the downregulation of the protease SpeB. (asm.org)
  • Importantly, however, we observed a differential impact of EndoS-mediated sugar side chain hydrolysis on IgG activity depending on the individual IgG subclass. (pnas.org)
  • Saturation of cellular antibody receptors by endogenous antibody limits antibody-dependent cell-mediated cytotoxicity (ADCC) and antibody dependent cellular phagocytosis (ADCP). (hansamedical.com)
  • Here we show how enzymatic cleavage of IgG using the bacterial enzyme IdeS can be utilized to empty both high and low affinity Fcγ-receptors and clear the entire endogenous antibody pool. (hansamedical.com)
  • Phylogenetic analyses indicate that the CaM-binding site is conserved in peroxisomal processing proteases of higher plants (dicots, monocots) but not present in orthologs of animals or cellular slime molds. (springer.com)
  • These results demonstrate that although the proteasome and calpain protease systems are capable of degrading tau in cell-free assays, their inhibition does not alter cellular tau levels in primary neurons or differentiated neuroblastoma cells. (semcs.net)
  • Our studies thus reveal an important role for pathogen-mediated modification of cellular kinases as a potential strategy for bacterial persistence within target host cells, which is associated with low-grade chronic inflammation, a hallmark of pathogen-mediated chronic inflammatory disorders. (nih.gov)
  • These proteases are found to localize in different cellular compartments. (asm.org)
  • By comparing intramembrane proteases in different cellular organelles, we set out to review their functions within the context of the roles of individual cellular compartments. (biologists.org)
  • With the exception of peroxisomes, at least one intramembrane protease is found in every membrane-enclosed cellular compartment (see poster). (biologists.org)
  • The human degradome, which makes up a complete list of proteases synthesized by human cells, is made up of at least 569 proteases that are distributed into five broad classes (in order from greatest to least number): metalloproteinases, serine, cysteine, threonine, and aspartic proteases [ 2 ]. (thno.org)
  • An immunization survey of human serum samples suggests that exposure to S. aureus glutamyl endopeptidase is common, although a correlation to any specific type of infection could not be established. (wikipedia.org)
  • The level of internalization of parasites treated with the anti-115-kDa antibody into host macrophages was significantly reduced from that of non-antibody-treated parasites, suggesting that this serine protease probably plays a role in the infection process. (asm.org)