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.
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.
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.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
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.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
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.
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
An essential amino acid that is required for the production of HISTAMINE.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
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.
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Enzymes which catalyze the hydrolysis of carboxylic acid esters with the formation of an alcohol and a carboxylic acid anion.
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.
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).
One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.
The rate dynamics in chemical or physical systems.
Any member of the class of enzymes that catalyze the cleavage of the substrate and the addition of water to the resulting molecules, e.g., ESTERASES, glycosidases (GLYCOSIDE HYDROLASES), lipases, NUCLEOTIDASES, peptidases (PEPTIDE HYDROLASES), and phosphatases (PHOSPHORIC MONOESTER HYDROLASES). EC 3.
The process of cleaving a chemical compound by the addition of a molecule of water.
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
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.
Peptide hydrolases that contain at the active site a SERINE residue involved in catalysis.
Proteins prepared by recombinant DNA technology.
An enzyme that catalyzes the hydrolysis of a single fatty acid ester bond in lysoglycerophosphatidates with the formation of glyceryl phosphatidates and a fatty acid. EC 3.1.1.5.
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
An enzyme that catalyzes the conversion of acetate esters and water to alcohols and acetate. EC 3.1.1.6.
A di-isopropyl-fluorophosphate which is an irreversible cholinesterase inhibitor used to investigate the NERVOUS SYSTEM.
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.
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.
A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. It also hydrolyzes peptide amides. (From Enzyme Nomenclature, 1992) EC 3.4.21.62.
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.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
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.
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)
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.
Proteins found in any species of bacterium.
An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. It is produced by glands on the tongue and by the pancreas and initiates the digestion of dietary fats. (From Dorland, 27th ed) EC 3.1.1.3.
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.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.
Carboxylesterase is a serine-dependent esterase with wide substrate specificity. The enzyme is involved in the detoxification of XENOBIOTICS and the activation of ester and of amide PRODRUGS.
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.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
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.
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.
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.
A condition of competitive female athletes in which there are interrelated problems of EATING DISORDERS; AMENORRHEA; and OSTEOPOROSIS.
A subclass of exopeptidases that includes enzymes which cleave either two or three AMINO ACIDS from the end of a peptide chain.
A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
A subclass of EXOPEPTIDASES that act on the free N terminus end of a polypeptide liberating a single amino acid residue. EC 3.4.11.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
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.
A genus of gram-negative, aerobic, rod-shaped bacteria found in wet soil containing decaying organic material and in water. Cells tend to be pleomorphic if grown on media containing succinate or coccoid if grown in the presence of an alcohol as the sole carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
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.
A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
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.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
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.
Peptides composed of two amino acid units.
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.
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.
Proteins found in the PERIPLASM of organisms with cell walls.
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.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
A plant genus of the family EUPHORBIACEAE, order Euphorbiales, subclass Rosidae. Commercial natural RUBBER is mainly obtained from Hevea brasiliensis but also from some other plants.
An enzyme that catalyzes the transfer of acetyl groups from ACETYL-COA to arylamines. It can also catalyze acetyl transfer between arylamines without COENZYME A and has a wide specificity for aromatic amines, including SEROTONIN. However, arylamine N-acetyltransferase should not be confused with the enzyme ARYLALKYLAMINE N-ACETYLTRANSFERASE which is also referred to as SEROTONIN ACETYLTRANSFERASE.
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.
Compounds containing the -SH radical.
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.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
A group of enzymes that catalyze the hydrolysis of diphosphate bonds in compounds such as nucleoside di- and tri-phosphates, and sulfonyl-containing anhydrides such as adenylylsulfate. (Enzyme Nomenclature, 1992) EC 3.6.
A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.
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.
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.
Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). It uses a catalytic triad of Cysteine ... Asparagine endopeptidase is synthesized as an inactive zymogen. AEP and other cysteine peptidase are activated when pH changes ... hence also called cysteine protease). It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 ... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Letters. 441 (3): 361-5. doi:10.1016/S0014-5793(98) ...
These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. ... Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... See also: catalytic triad. The first step in the reaction mechanism by which cysteine proteases catalyze the hydrolysis of ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ...
Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). Catalysis is achieved by one of two mechanisms: ... One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or ... Ligase Protease cysteine- serine- threonine- aspartic- glutamic- metallo- PA clan Convergent evolution Proteolysis Catalytic ...
... (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine ... TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed ... P2-Phe is also surrounded by hydrophobes including the face of the triad histidine; P1-Gln forms four hydrogen bonds; and P1'- ... Dougherty WG, Parks TD, Cary SM, Bazan JF, Fletterick RJ (September 1989). "Characterization of the catalytic residues of the ...
The catalytic cleft is formed by PC1 and PC2 upon calcium binding. The catalytic triad consists of residues C105, H262, and ... This enzyme catalyses the following chemical reaction Broad endopeptidase specificity This enzyme belongs to the peptidase ... is an intracellular heterodimeric calcium-activated cysteine protease. ... Calpain-2 is a heterodimer of a catalytic subunit encoded by CAPN2 gene and a regulatory subunit CAPNS1. The catalytic subunit ...
... which contains a catalytic dyad that has been likened to the catalytic triad of chymotrypsin. The catalytic dyad is made up of ... A nearby Asn-175 helps to orient the imidazole ring of His-159 to allow it to deprotonate the catalytic Cys-25. This cysteine ... including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endopeptidase activity. Members ... Aspartate-158 was thought to play a role analogous to the role of aspartate in the serine protease catalytic triad, but that ...
... three amino acid residues work together to form a catalytic triad which makes up the catalytic site. In chymotrypsin, these ... there are two cysteine residues besides the FAD cofactor and are used to break the disulphide bond during the catalytic ... Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide. It ... The catalytic process starts when the FAD is reduced by NADPH to accept one electron and from FADH−. It then attacks the ...
These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine+endopeptidases at the US National ... Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the ... Within each superfamily, families are designated by their catalytic nucleophile (C denoting cysteine proteases). The first step ...
Their mechanism of action relies on undergoing a large conformational change which inactivates their target's catalytic triad. ... This domain is also found, in one or more copies, in a variety of cysteine peptidase inhibitors such as salarin. The ... This family includes PinA, which inhibits the endopeptidase La. It binds to the La homotetramer but does not interfere with the ... It has no similarity to any other known cysteine proteinase inhibitors but bears some similarity to a lectin-like family of ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... serine-type endopeptidase activity. Cellular component. • lamellipodium membrane. • extracellular exosome. • lysosomal membrane ...
One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). ... Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ... See also: Catalytic triad. Proteases are involved in digesting long protein chains into shorter fragments by splitting the ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... positive regulation of catalytic activity. • neutrophil degranulation. • negative regulation of chaperone-mediated autophagy. ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ...
All of them are cysteine proteases with a chymotrypsin-like fold (PA clan), using a catalytic dyad or triad. They share some ... The 3C-like protease (3CLpro) or Mpro, formally known as C30 Endopeptidase, is the main protease found in coronaviruses. It ... It is a cysteine protease and a member of the PA clan of proteases. It has a cysteine-histidine catalytic dyad at its active ... The 3CL protease has a cysteine-histidine catalytic dyad at its active site. The sulfur of the cysteine acts as a nucleophile ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate ... Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised.[1] More recently, ... Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are synthesised with signal and propeptides. The animal ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... endopeptidase activity. • amyloid-beta binding. • beta-aspartyl-peptidase activity. • GO:0001948 protein binding. • enzyme ... aspartic-type endopeptidase activity. Cellular component. • multivesicular body. • late endosome. • endoplasmic reticulum lumen ...
These three amino acids are known as the catalytic triad which means that these three must all be present in order to properly ... Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that bond. Three common ... Disulfide bond formation is the creation of disulfide bridges (covalent bonds) between two cysteine amino acids in a chain ... Non-covalent interactions such as hydrogen bonding between the peptide backbone and the catalytic triad help increase reaction ...
This is possible due to the catalytic triad in their active site of their protein sequence: Aspartate, Serine and Histidine ( ... The carboxyl terminus of the last cysteine forms a hydrogen bond with the N terminus. This interaction allows the stabilization ... "AmiGO 2: Term Details for "serine-type endopeptidase activity" (GO:0004252)". Amigo. Gene Ontology Consortium. Retrieved 2018- ... the triad is presented in this specific order in the S8 family). The serine nucleophile responsible for the cleave of peptide ...
These three amino acids are known as the catalytic triad which means that these three must all be present in order to properly ... Cysteine HS-CH2- Serine → Cystathionine → α-ketobutyrate → Cysteine Asparagine H2N-CO-CH2- Aspartic Acid → Asparagine ( ... EndopeptidasesEdit. Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that ... Non-covalent interactions such as hydrogen bonding between the peptide backbone and the catalytic triad help increase reaction ...
Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... Proteasome endopeptidase complex (EC 3.4.25.1, ingensin, macropain, multicatalytic endopeptidase complex, prosome, ... Proteasome+endopeptidase+complex at the US National Library of Medicine Medical Subject Headings (MeSH) ...
The enzyme TEV protease contains a catalytic triad of residues (red) in its catalytic site. The substrate (black) is bound by ... there are two cysteine residues besides the FAD cofactor and are used to break the disulphide bond during the catalytic ... Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide.[1] ... three amino acid residues work together to form a catalytic triad which makes up the catalytic site. In chymotrypsin, these ...
Serine hydrolase Protease cysteine- threonine- aspartic- metallo- PA clan Convergent evolution Proteolysis Catalytic triad The ... Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the ... The main player in the catalytic mechanism in the serine proteases is the catalytic triad. The triad is located in the active ... but shares the same catalytic mechanism utilising a catalytic triad, to create a nucleophilic serine. This is the classic ...
cysteine-type endopeptidase activity. • cysteine-type peptidase activity. • hydrolase activity. Cellular component. • lysosome ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific ... 1998). "Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase". Leukemia. 12 (11): 1771-81. doi: ...
... 's endopeptidase activity is primarily responsible for the catalytic process of selectively cleaving Gln-Gly bonds ... selective crystallization and formation of a functional catalytic triad in the active site". Journal of Molecular Biology. 354 ... Picornain 3C are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ... Hepatitis A 3C proteinase is a member of the cysteine proteases that are responsible for the infectivity and maturation of HAV ...
cysteine-type endopeptidase activity involved in apoptotic process. • tumor necrosis factor receptor binding. • cysteine-type ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... cysteine-type peptidase activity. • cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • protein ... cysteine-type endopeptidase activity involved in execution phase of apoptosis. Cellular component. • cell body. • cytosol. • ...
activation of cysteine-type endopeptidase activity involved in apoptotic process. • response to drug. • signal transduction. • ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... Each protein is divided into three domains: an N-terminal extracellular domain with four cadherin-like repeats and a cysteine- ...
serine-type endopeptidase activity. • cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. ... The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and ... Lenarcic B, Kos J, Dolenc I, Lucovnik P, Krizaj I, Turk V (July 1988). "Cathepsin D inactivates cysteine proteinase inhibitors ...
Since ricin is a catalytic irreversible inhibitor, this allows just a single molecule of ricin to kill a cell.[56] ... This reactive form of DFMO then reacts with either a cysteine or lysine residue in the active site to irreversibly inactivate ... However, this decarboxylation reaction is followed by the elimination of a fluorine atom, which converts this catalytic ... except that the EIS complex has catalytic activity, which may be lower or even higher (partially competitive activation) than ...
Catalytic mechanism[edit]. There are three catalytic mechanisms published. *In the first mechanism, Browner M.F. and colleagues ... The pro-peptide domain is part of the "cysteine switch." This contains a conserved cysteine residue that interacts with the ... They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade ... The catalytic domain[edit]. X-ray crystallographic structures of several MMP catalytic domains have shown that this domain is ...
Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a ... peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core [ ... There is a catalytic triad which occurs in the order: Cys/His/Asn (or Asp). A fourth residue, usually Gln, is important for ... A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ...
Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a ... Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... There is a catalytic triad which occurs in the order: Cys/His/Asn (or Asp). A fourth residue, usually Gln, is important for ... A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ...
These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. ... Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... See also: catalytic triad. The first step in the reaction mechanism by which cysteine proteases catalyze the hydrolysis of ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ...
Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). It uses a catalytic triad of Cysteine ... Asparagine endopeptidase is synthesized as an inactive zymogen. AEP and other cysteine peptidase are activated when pH changes ... hence also called cysteine protease). It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 ... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Letters. 441 (3): 361-5. doi:10.1016/S0014-5793(98) ...
Catalytic Domain / physiology * Crystallization * Cysteine Endopeptidases / metabolism* * Endopeptidases / genetics * ... Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad ... Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin ...
... papain-like cysteine protease) in MEROPS (the Peptidase Database). The 3D structure and substrate specificity of the zmCP1 is ... Cysteine protease 1 precursor from Zea mays (zmCP1) is classified as a member of the C1A family of peptidases ( ... The catalytic triad consists of two amino acids-cysteine and histidine. Aspartyl was concluded to play a role analogous to ... The S2 pocket is the major determinant of specificity for most cysteine proteinases [13]. KDEL-tailed cysteine endopeptidase ( ...
TEV protease (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine ... TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed ... P2-Phe is also surrounded by hydrophobes including the face of the triad histidine; P1-Gln forms four hydrogen bonds; and P1- ... Dougherty WG, Parks TD, Cary SM, Bazan JF, Fletterick RJ (September 1989). "Characterization of the catalytic residues of the ...
... residue in their active side and therefore employ the sulfhydryl group of the side chain of a cysteine residue as the catalytic ... A catalytic dyad of Cys and His is employed by clan CD whereas a catalytic triad of Cys, His, and Asn is used by clan CA ... Cathepsin B is a lysosomal cysteine protease with both endopeptidase and dipeptidyl carboxypeptidase activities. The substrate ... Clan CA Cysteine Proteases. The majority of cysteine proteases belong to clan CA and these cysteine proteases have been found ...
Although the catalytic core geometry shows evolutionary divergence between taxa, the relative positions of the catalytic triad ... The PA clan of endopeptidases is the most abundant and over two thirds of this clan is comprised of the S1 family of serine ... in alternating colors and cysteine residues Cys 267 (blue) and Cys287 (red) forming a predicted disulfide bond (2.04 Å). Table ... that together form what is referred to as the catalytic triad (or a dyad in some cases) [2]. The presence of this catalytic ...
histidine triad. AW418666. catalytic activity. nucleotide. HINT3. binding protein 3. TIP41, TOR. NM_152902.1. protein binding. ... endopeptidase. membrane. (apollon). inhibitor activity. fraction. anti-apoptosis. cysteine protease. inhibitor activity. ... All isoforms except PKC α, β1, β2, and γ lack the C2 domain, and the λ, η isoforms also lack nine of two cysteine-rich zinc ... Homo sapiens protein kinase, AMP-activated, beta 2 non-catalytic. NM_005399.1/DEF. 72. ...
displays a minimal thiol-protease fold and its catalytic triad; potential redox regulation: the catalytic cysteine can form a ... IgG-specific endopeptidase IdeS (Sib38) [117762] (1) *Lpg0564-like [142864] (1) Pfam 07313, DUF1460; contains new PDB entry ... consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn *Superfamily ... Pfam 09641; DUF2026; putative Cys/Ser-His-Asp catalytic triad *M48USP-like [159852] (1) Pfam 04843; Herpesvirus tegument ...
Although the catalytic core geometry shows evolutionary divergence between taxa, the relative positions of the catalytic triad ... The PA clan of endopeptidases is the most abundant and over two thirds of this clan is comprised of the S1 family of serine ... there are several viral PA proteases that alternatively use a nucleophilic cysteine (Cys) residue (C sub-clan) [5]. However, ... that together form what is referred to as the catalytic triad (or a dyad in some cases) [2]. The presence of this catalytic ...
The NlpC/P60 domain is a primitive cysteine protease which contains a Cys126/His176/His188 triad and a conserved catalytic core ... 4. Structure of the-D-glutamyl-L-diamino acid endopeptidase YkfC from Bacillus cereus in complex with L-Ala--D-Glu: insights ... Structural Evidence for a Novel Cysteine Peptidase Catalytic Triad. JM Aramini, P Rossi, YJ Huang, L Zhao, M Jiang - ... into the functions of SH3b domain and the catalytic domain and how substrate specificity is achieved for this class of cysteine ...
It has been observed that cloning, expression and purification of proteases often fail due to their catalytic functions which, ... Cysteine proteases use a similar catalytic triad as serine proteases except that a cysteine residue is recognized instead of ... Endopeptidases may be further sub-divided into four types according to their catalytic mechanism: serine, cysteine, aspartic ... Carter P, Wells JA: Dissecting the catalytic triad of a serine protease. Nature. 1988, 332 (6164): 564-568. 10.1038/332564a0. ...
Ser-His Asp Catalytic Triad. covalent intermediate. Cysteine. Cys-His. covalent intermediate ... endopeptidase. exopeptidase. Two types of cleavages. Same rxn, Four mechanisms. Named for residue/group in active site of ...
The Z-Ala-Ala-AzaAsn-cmk inhibitor (purple sticks) is covalently linked to the catalytic Cys189. The catalytic triad is ... Full endopeptidase activity can be obtained by pH reduction to pH 4.0 (2⇓-4). The acidification is accompanied by ... 1999) Crystal structure of gingipain R: An Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J 18(20): ... His148 (Hisc237) and Asn42 complete the catalytic triad (Oδ1Asn42-Nε2His148 ∼3.0 Å; Fig. 1B). Interestingly, caspases exhibit a ...
The three conserved catalytic residues of this superfamily are shown to be equivalent to the catalytic triad of the papain-like ... We identified three conserved residues, namely a cysteine, a histidine and a polar residue, that are involved in the catalytic ... Several related, but distinct, catalytic activities, such as murein degradation, acyl transfer and amide hydrolysis, have ... These eukaryotic proteins, along with the bacterial YaeF/poxviral G6R family, show a circular permutation of the catalytic ...
Aligned side chains of serine, histidine and aspartate build the catalytic triad common to most serine proteases. ... alpha-lytic endopeptidase, glutamyl endopeptidase (V8), protease Do (htrA) (Escherichia), togavirin, lysyl endopeptidase, IgA- ... Cysteine, threonine or water molecules associated with aspartate or metals may also play this role. In many cases, the ... specific serine endopeptidase, flavivirin, hepatitis C virus NS3 endopeptidase, tobacco etch virus 35 Kd endopeptidase, cattle ...
The first crystal structure of an active plant asparaginyl endopeptidase reveals a tetrahedral intermediate state in its active ... This hypothesis is supported by the low level of endopeptidase activity observed with Ala mutations of the catalytic His in ... Intrinsic evolutionary constraints on protease structure, enzyme acylation, and the identity of the catalytic triad * AR Buller ... The current work presents the first structure of an "active" cysteine protease asparaginyl endopeptidase (AEP) that is capable ...
Catalytic activity. Reaction=Endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-,-Xaa and the ... The CV 3CLpro domain is predicted to contain a catalytic triad constituted of His, Asp and Cys residues, where the Cys likely ... This polyprotein processing is carried out by a 3C-like cysteine protease (3CLpro). ...
... peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core. We ... Structural basis of murein peptide specificity of a γ-D-glutamyl-l-diamino acid endopeptidase Academic Article ... The crystal structures of two homologous endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme were ... that these two proteins act as gamma-D-glutamyl-L-diamino acid endopeptidases (EC 3.4.22.-). The active site is located near ...
... serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in ... but shares the same catalytic mechanism utilising a catalytic triad, to create a nucleophilic serine. This is the classic ... Endopeptidase 3.4.21-24. Serine proteases - Cysteine protease - Aspartic acid protease - Metalloendopeptidases. ... Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21). Digestive system. Enteropeptidase - Trypsin - Chymotrypsin ...
... cysteine-, aspartic-, serine-, and metallo-peptidases), cell, protein and lipid binding including mucins and iron/heme ... catalytic aa in the trypsin catalytic triad were conserved (Figure 13). Additionally, although we were only able to sequence ... Arrowheads indicate the catalytic cysteine motif. Shading represents 100% identity (black) or similarity (grey) among the ... Analysis of aspartic endopeptidases (AE), a legumain-like family of proteins. (A) Phylogenetic tree based on maximum likelihood ...
Amino Acid Sequence, Catalysis, Catalytic Domain, Cysteine, Cysteine Endopeptidases, Escherichia coli, Escherichia coli ... The active site features a novel Cys-His-His catalytic triad that appears to be a unique structural signature of this cysteine ... structural evidence for a novel cysteine peptidase catalytic triad. Title. Solution NMR structure of the NlpC/P60 domain of ... structural evidence for a novel cysteine peptidase catalytic triad.. ...
Ball and stick representation shows the conserved catalytic triad and other important residues. The figure is colored as in ... Cysteine Endopeptidases/chemistry*. *Drug Design. *Kinetics. *Malaria, Falciparum/drug therapy. *Malaria, Falciparum/enzymology ... Cysteine proteases of the papain superfamily are implicated in a number of cellular processes and are important virulence ... We report the crystal structures of three major parasite cysteine proteases, cruzain, falcipain-3, and the first reported ...
Cysteine , Endopeptidase K/chemistry , Fungal Proteins/chemistry , Hydrogen Bonding , Mercury/pharmacology , Molecular ... binding of mercury distorts the stereochemistry of the neighbouring residues including those belonging to the catalytic triad. ...
Proteases are classified according to their catalytic site, and distributed into four major classes: cysteine proteases, serine ... cysteine proteases, serine proteases, aspartic proteases and metallo-proteases. This review will cover only cysteine proteases ... Cysteine protease inhibitors are available that can block the active site but no such inhibitor available yet that can be ... Cysteine protease inhibitors are available that can block the active site but no such inhibitor available yet that can be ...
The hydrogen bonding system of the catalytic triad remained intact after the treatment. However, the water structure in the ... Cysteine , Endopeptidase K/chemistry , Fungal Proteins/chemistry , Hydrogen Bonding , Mercury/pharmacology , Molecular ... Enhancement of catalytic activity of enzymes by heating in anhydrous organic solvents: 3D structure of a modified serine ... binding of mercury distorts the stereochemistry of the neighbouring residues including those belonging to the catalytic triad. ...
One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or ... endopeptidases, such as trypsin, chymotrypsin, pepsin, papain, elastase). ... Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ... See also: Catalytic triad. Proteases are involved in digesting long protein chains into shorter fragments by splitting the ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... Catalytic triad. *Oxyanion hole. *Enzyme promiscuity. *Catalytically perfect enzyme. *Coenzyme. *Cofactor. *Enzyme catalysis ... serine-type endopeptidase activity. Cellular component. • lamellipodium membrane. • extracellular exosome. • lysosomal membrane ...
  • Cysteine proteases , also known as thiol proteases , are enzymes that degrade proteins . (wikipedia.org)
  • These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. (wikipedia.org)
  • Cysteine proteases are commonly encountered in fruits including the papaya , pineapple , fig and kiwifruit . (wikipedia.org)
  • In fact, dozens of latices of different plant families are known to contain cysteine proteases. (wikipedia.org)
  • [1] Cysteine proteases are used as an ingredient in meat tenderizers . (wikipedia.org)
  • For superfamilies , P = superfamily containing a mixture of nucleophile class families, C = purely cysteine proteases. (wikipedia.org)
  • Within each superfamily, families are designated by their catalytic nucleophile (C = cysteine proteases). (wikipedia.org)
  • The first step in the reaction mechanism by which cysteine proteases catalyze the hydrolysis of peptide bonds is de protonation of a thiol in the enzyme 's active site by an adjacent amino acid with a basic side chain , usually a histidine residue. (wikipedia.org)
  • Cysteine proteases play multi-faceted roles, virtually in every aspect of physiology and development. (wikipedia.org)
  • The ability of macrophages and other cells to mobilize elastolytic cysteine proteases to their surfaces under specialized conditions may also lead to accelerated collagen and elastin degradation at sites of inflammation in diseases such as atherosclerosis and emphysema . (wikipedia.org)
  • Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). (wikipedia.org)
  • TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases). (wikipedia.org)
  • Cysteine proteases have a cysteine residue in their active side and therefore employ the sulfhydryl group of the side chain of a cysteine residue as the catalytic nucleophile. (creativebiomart.net)
  • Some of the cysteine proteases use an extra amino acid to provide additional stabilization via hydrogen bonds, thus forming a catalytic triad. (creativebiomart.net)
  • Cysteine proteases currently consist of 10 clans. (creativebiomart.net)
  • We will focus on clan CA and clan CD cysteine proteases since the inhibitors reported in this thesis are designed for the enzymes belong to these two clans. (creativebiomart.net)
  • Clan CA and clan CD cysteine proteases differ slightly in their substrate hydrolysis mechanism. (creativebiomart.net)
  • A catalytic dyad of Cys and His is employed by clan CD whereas a catalytic triad of Cys, His, and Asn is used by clan CA cysteine proteases. (creativebiomart.net)
  • Stabilization of the tetrahedral intermediate occurs by H bonding to the backbone NH of active site Cys and to the NH2 group of the Gln side chain in clan CA. The oxyanion hole consists of only backbone NH groups in clan CD cysteine proteases. (creativebiomart.net)
  • The majority of cysteine proteases belong to clan CA and these cysteine proteases have been found in viruses, bacteria, protozoa, plants and mammals. (creativebiomart.net)
  • Calpains are a unique family of cysteine proteases since they require calcium to become activated. (creativebiomart.net)
  • 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)
  • The proteolytic mechanism of these proteases involves nucleophilic attack of the carbonyl atom of the substrate peptide bond by a catalytic serine (Ser) residue in the active site of the enzyme. (pubmedcentralcanada.ca)
  • The MEROPS classification system ( http://merops.sanger.ac.uk/ ) has grouped proteases into clans that typically have structural homology and/or the same linear order of catalytic triad residues [ 4 ]. (pubmedcentralcanada.ca)
  • Of all serine proteases, the PA clan of endopeptidases is the most abundant and has been studied the most in-depth. (pubmedcentralcanada.ca)
  • Although most members of this clan utilize a nucleophilic Ser residue (S sub-clan), there are several viral PA proteases that alternatively use a nucleophilic cysteine (Cys) residue (C sub-clan) [ 5 ]. (pubmedcentralcanada.ca)
  • It has been observed that cloning, expression and purification of proteases often fail due to their catalytic functions which, in turn, cause toxicity in the E. coli heterologous host. (biomedcentral.com)
  • Endopeptidases may be further sub-divided into four types according to their catalytic mechanism: serine, cysteine, aspartic and metallo proteases. (biomedcentral.com)
  • 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)
  • Cysteine proteases of the papain superfamily are implicated in a number of cellular processes and are important virulence factors in the pathogenesis of parasitic disease. (nih.gov)
  • We report the crystal structures of three major parasite cysteine proteases, cruzain, falcipain-3, and the first reported structure of rhodesain, in complex with a class of potent, small molecule, cysteine protease inhibitors, the vinyl sulfones. (nih.gov)
  • These data, in conjunction with comparative inhibition kinetics, provide insight into the molecular mechanisms that drive cysteine protease inhibition by vinyl sulfones, the binding specificity of these important proteases and the potential of vinyl sulfones as antiparasitic drugs. (nih.gov)
  • Proteases are classified according to their catalytic site, and distributed into four major classes: cysteine proteases, serine proteases, aspartic proteases, and metalloproteases. (frontiersin.org)
  • This review will cover only cysteine proteases, papain family enzymes which are involved in multiple functions such as extracellular matrix turnover, antigen presentation, processing events, digestion, immune invasion, hemoglobin hydrolysis, parasite invasion, parasite egress, and processing surface proteins. (frontiersin.org)
  • For preventing unwanted digestion, cysteine proteases are synthesized as zymogens, and contain a prodomain (regulatory) and a mature domain (catalytic). (frontiersin.org)
  • This review specifically highlights the modes of activation (processing) of papain family enzymes, which involve auto-activation, trans -activation and also clarifies the future aspects of targeting PPIs to prevent the activation of cysteine proteases. (frontiersin.org)
  • Cysteine proteases are present in all living organisms. (frontiersin.org)
  • Papain and cathepsins belong to the most abundant family of the cysteine proteases. (frontiersin.org)
  • In mammals, a main group of cysteine proteases is known as lysosomal cathepsins ( McGrath, 1999 ). (frontiersin.org)
  • P. falciparum expresses four papain-like cysteine proteases named as falcipain-1, 2, 2′ and 3. (frontiersin.org)
  • Proteases have evolved multiple times , and different classes of protease can perform the same reaction by completely different catalytic mechanisms . (wikipedia.org)
  • Proteases were first grouped into 84 families according to their evolutionary relationship in 1993, and classified under four catalytic types: serine, cysteine, aspartic, and metallo proteases. (wikipedia.org)
  • The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine (proteases) or a water molecule ( aspartic acid , metallo- and acid proteases) nucleophilic so that it can attack the peptide carboxyl group. (wikipedia.org)
  • [4] In this database, proteases are classified firstly by 'clan' ( superfamily ) based on structure, mechanism and catalytic residue order (e.g. the PA clan where P indicates a mixture of nucleophile families). (wikipedia.org)
  • Of these families, the largest contingent comprises serine proteases, which are named based on their application of the hydroxyl group of a serine side chain as catalytic nucleophile. (schoolbag.info)
  • Yet, other serine proteases present novel catalytic triads, such as a pair of histidines combined with the nucleophilic serine. (schoolbag.info)
  • Chemical biological approaches are used or are being developed to study the substrate specificity, catalytic mechanism and biological role of proteases and their macromolecular inhibitors. (ucsf.edu)
  • The genes for serine (trypsin, serine collagenase, easter, prostate specific antigen, T-cell specific granzymes, MT-SP1 and 2, KSHV protease), cysteine (cruzain and falcipain) and aspartyl (HIV1 & HIV2 & SIV) proteases and macromolecular inhibitors such as ecotin and single chain antibodies are manipulated and expressed in heterologous expression systems. (ucsf.edu)
  • Sequence alignment of C13 family of cysteine proteases. (elifesciences.org)
  • Contains a highly conserved catalytic triad of Ser-type proteases (Ser-His-Asp). (gifu-u.ac.jp)
  • Although the overall fold of various serine proteases may differ, they all follow the same mechanism of action through an identical stereochemistry of the catalytic triad and oxyanion hole. (springer.com)
  • 7] In this database, proteases are classified firstly by 'clan' (superfamily) based on structure, mechanism and catalytic residue order (e.g. (kiev.ua)
  • Mesophilic alkaline serine proteases from various bacteria have been commercially applied in a range of industries owing to their high catalytic efficiency and wide substrate specificity. (biomedcentral.com)
  • However, these proteases have an optimal catalytic temperature of approximately 50 °C, and their activity decreases significantly at low temperature. (biomedcentral.com)
  • Therefore, to enhance their cold activity, it is necessary to improve the catalytic performance of these proteases at low temperature. (biomedcentral.com)
  • Therefore, bacterial serine proteases have been extensively characterized in terms of their catalytic mechanisms [ 3 , 4 ]. (biomedcentral.com)
  • The proteases from mesophilic bacteria usually exhibit higher catalytic efficiency at 45-50 °C, and their activity decreases rapidly at low temperature. (biomedcentral.com)
  • Unlike soluble proteases, the catalytic heart of these enzymes appears buried within the lipid bilayer, an unexpected location for a hydrolytic reaction, which requires water. (embopress.org)
  • The around 100 DUB enzymes could be grouped into five primary classes composed of the cysteine proteases ubiquitin C-terminal hydrolases (UCHs) ubiquitin-specific proteases (USPs) ovarian tumor proteases (OTUs) and Machado-Joseph area proteases (MJDs) as well as the metalloproteases JAB1/MPN/MOV34 (JAMM) 6. (morainetownshipdems.org)
  • these cysteine proteases comprise the largest sub-group of deubiquitinase enzymes (DUBs). (atlasgeneticsoncology.org)
  • Comparative sequence and structural analysis, particularly to penicillin V acylase (MEROPS peptidase family C59) revealed a cysteine as the catalytic nucleophile as well as other conserved residues important for catalysis [ PMID: 12717035 ]. (ebi.ac.uk)
  • Binding by ubiquitin aldehyde induces a drastic conformational change in the active site that realigns the catalytic triad residues for catalysis. (nih.gov)
  • The structural geometry of the catalytic core shows clear deviations between taxa, but the relative positions of the catalytic triad residues were conserved. (pubmedcentralcanada.ca)
  • We identified three conserved residues, namely a cysteine, a histidine and a polar residue, that are involved in the catalytic activities of this superfamily. (biomedcentral.com)
  • The three conserved catalytic residues of this superfamily are shown to be equivalent to the catalytic triad of the papain-like thiol peptidases. (biomedcentral.com)
  • By substituting catalytic residues we could alter the ratio of cyclic to acyclic products. (elifesciences.org)
  • The CV 3CLpro domain is predicted to contain a catalytic triad constituted of His, Asp and Cys residues, where the Cys likely represents the nucleophilic residue and Asp the acidic residue. (expasy.org)
  • Moreover, the relative orientation of these catalytic residues is similar to that observed in the analogous Ser-His-His triad, a variant of the classic Ser-His-Asp charge relay system, suggesting the convergent evolution of a catalytic mechanism in quite distinct peptidase families. (rostlab.org)
  • The active sites of cruzain ( A ), rhodesain ( B ), and falcipain-3 ( C ). Ball and stick representation shows the conserved catalytic triad and other important residues. (nih.gov)
  • [3] During this reaction, the catalytic asparagine forms a cyclic chemical structure that cleaves itself at asparagine residues in proteins under the right conditions. (wikipedia.org)
  • Here, the crystal structure of PPAF‐II reveals that the clip domain adopts a novel fold containing a central cleft, which is distinct from the structures of defensins with a similar arrangement of cysteine residues. (embopress.org)
  • A ) Catalytic residues with dual conformations illustrated in the HaAEP1 active site with simulated annealing omit electron density maps (2 F obs - F calc ) contoured at 1σ level. (elifesciences.org)
  • It cleaves efficiently after hydrophobic residues, fails to cleave before or after proline residues, and displays endopeptidase activity by cleaving after lysine residues, although this activity is weak when compared to its exopeptidase function [ 3 , 12 ]. (hindawi.com)
  • A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. (ebi.ac.uk)
  • Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. (ebi.ac.uk)
  • EC 3.4.22.34) is a proteolytic enzyme from C13 peptidase family which hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile (hence also called cysteine protease). (wikipedia.org)
  • Substrate access and turnover is controlled by selective protonation of the S1 pocket ( K M ) and the catalytic nucleophile ( k cat ), respectively. (pnas.org)
  • One way to make a nucleophile is by a catalytic triad , where a histidine residue is used to activate serine , cysteine , or threonine as a nucleophile. (wikipedia.org)
  • Sortases catalyze transpeptidation using a conserved active site His-Cys-Arg triad that joins a sorting signal located at the C terminus of their protein substrate to an amino nucleophile located on the cell surface. (anl.gov)
  • Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. (ebi.ac.uk)
  • 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. (ebi.ac.uk)
  • In this step, a fragment of the substrate is released with an amine terminus, the histidine residue in the protease is restored to its deprotonated form, and a thioester intermediate linking the new carboxy-terminus of the substrate to the cysteine thiol is formed. (wikipedia.org)
  • A catalytic dyad is formed with the imidazole side chain of histidine residue and the sulfhydryl group of the active site cysteine. (creativebiomart.net)
  • In addition to the nucleophilic Ser residue, this reaction is dependent on two other amino acids in the catalytic site, Histidine (His) and an Aspartate (Asp) that together form what is referred to as the catalytic triad (or a dyad in some cases) [ 2 ]. (pubmedcentralcanada.ca)
  • Expanded surface and cartoon representations of highlighted regions of β IV -β V substrate binding region (blue backgrounds) and catalytic region (β I sheet, β5-β IV loop and β I -β III region) orientated over the catalytic His residue (yellow backgrounds) are shown below illustrating the residue differences that could alter substrate specificity (shown in stick format). (elifesciences.org)
  • The typical REC active pocket structure consists of an 'acidic triad' that includes the phospho-accepting Asp residue at the end of the β3 strand and two other acidic amino acids within the β1-α1 loop, an 'invariant' lysine (Lys) residue at the end of the β5 strand and a metal ion (usually Mg 2+ ) that are coordinated through hydrogen bonding [ 4 ]. (prolekare.cz)
  • One contains a binding site for thrombin , another for high molecular weight kininogen , a third one for factor IX , heparin and glycoprotein Ib and the fourth is implicated in forming the factor XI homodimer, including a cysteine residue that creates a disulfide bond . (wikidoc.org)
  • Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism . (wikipedia.org)
  • Reaction mechanism of the cysteine protease mediated cleavage of a peptide bond. (wikipedia.org)
  • It is the first cysteine protease to be discovered and has been the subject of mechanism and structural studies for many years and it is also the first enzyme to have its crystal structure determined. (creativebiomart.net)
  • Substrate specificity and catalytic mechanism of legumain. (pnas.org)
  • 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)
  • The main player in the catalytic mechanism in the chymotrypsin and subtillisin clan enzymes mentioned above is the catalytic triad . (bionity.com)
  • However, despite extensive study, the catalytic mechanism and molecular basis of substrate recognition remains poorly understood. (anl.gov)
  • It should be noted that several serine protease families use a dyad mechanism in which lysine or histidine is paired with the catalytic serine. (schoolbag.info)
  • Since, unlike other 3D template approaches, the ETA method bypasses the need for experimental knowledge of the catalytic mechanism, it should prove a useful, large scale, and general adjunct to combine with other methods to decipher protein function in the structural proteome. (biomedcentral.com)
  • Finally, the possible mechanism responsible for the change in catalytic properties for these variants was interpreted based on structural modeling. (biomedcentral.com)
  • Kim, CU, "Structural insights into the effect of active-site mutation on the catalytic mechanism of carbonic anhydrase", IUCrJ 7: 985-994 (2020). (cornell.edu)
  • Endopeptidases cleave peptide bonds within the proteins. (biomedcentral.com)
  • These eukaryotic proteins, along with the bacterial YaeF/poxviral G6R family, show a circular permutation of the catalytic domain. (biomedcentral.com)
  • We deduced from structure and sequence analysis, and then experimentally, that these two proteins act as gamma-D-glutamyl-L-diamino acid endopeptidases (EC 3.4.22. (scripps.edu)
  • Sortase cysteine transpeptidases covalently attach proteins to the bacterial cell wall or assemble fiber-like pili that promote bacterial adhesion. (anl.gov)
  • In plants, protein hydrolysis via cysteine proteinases is thought to be modulated, at least in part, by a group of proteins called the cysteine proteinase inhibitors. (biomedcentral.com)
  • lang=en terms the difference between protease and proteinase is that protease is (enzyme) an enzyme that cuts or cleaves proteins while proteinase is (enzyme) protease. (kiev.ua)
  • Analysis of purified mutant proteins suggests that rhomboids use a serine protease catalytic dyad instead of the previously proposed triad. (embopress.org)
  • There is a catalytic dyad which occurs in the order His/Cys. (ebi.ac.uk)
  • The active site consists of a His/Cys catalytic dyad. (ebi.ac.uk)
  • These differences likely lead to variations in substrate specificity and catalytic efficiency among the three enzymes. (springer.com)
  • Several related, but distinct, catalytic activities, such as murein degradation, acyl transfer and amide hydrolysis, have emerged in the N1pC/P60 superfamily. (biomedcentral.com)
  • Mutagenesis of the aspartic acid to alanine impacts peptide bond hydrolysis to a greater extent than ester hydrolysis, which indicates that a complete catalytic triad is required for the hydrolysis of the stronger peptide bond. (schoolbag.info)
  • Cysteine protease 1 precursor from Zea mays (zmCP1) is classified as a member of the C1A family of peptidases (papain-like cysteine protease) in MEROPS (the Peptidase Database). (beds.ac.uk)
  • They were found to belong to the subtilisin family of enzymes and have been assigned as endopeptidase Q in the MEROPS database [ 18 ]. (biomedcentral.com)
  • The catalytic site of USPs include a triad using a catalytic cysteine and close by histidine and asparagine/aspartate to greatly help poise the cysteine for nucleophilic strike. (morainetownshipdems.org)
  • It is also known as asparaginyl endopeptidase, citvac, proteinase B, hemoglobinase, PRSC1 gene product or LGMN (Homo sapiens), vicilin peptidohydrolase and bean endopeptidase. (wikipedia.org)
  • Evolution has repeatedly recruited the Cys-protease asparaginyl endopeptidase (AEP) to perform their head-to-tail ligation. (elifesciences.org)
  • Focusing on the common core containing the catalytic site of the enzyme, this analysis is beneficial for future molecular modeling strategies and structural analysis of serine protease models. (pubmedcentralcanada.ca)
  • The triad is located in the active site of the enzyme, where catalysis occurs, and is preserved in all serine protease enzymes. (bionity.com)
  • section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes. (uniprot.org)
  • Many other enzyme families use the same catalytic triad, such as asparaginases, esterases, acylases, and β-lactamases (5). (schoolbag.info)
  • The other enzyme is a previously characterized midgut cathepsin L-like cysteine proteinase designated BmCL1. (biomedcentral.com)
  • For example, the P3C9 mutant of the mesophilic serine-like protease (SSII) from Bacillus sphaericus was constructed through molecular evolution and exhibited a 9.6-fold increase in catalytic efficiency ( k cat / K m ) compared with the wild-type (wt) enzyme [ 12 ]. (biomedcentral.com)
  • The presence of this catalytic triad in at least four distinct protein folds indicates evolutionary success in four different contexts [ 3 ]. (pubmedcentralcanada.ca)
  • others attack internal peptide bonds of a protein ( endopeptidases , such as trypsin , chymotrypsin , pepsin , papain , elastase ). (wikipedia.org)
  • In germinating mung bean seeds, it has been shown that at least two cysteine proteinases are induced soon after germination has started [ 15 ], and these authors proposed that vacuolar receptors (VCRs) transport these newly made proteinases to the protein storage vesicles (PSVs) thereby enabling them to participate in the mobilization of the seed protein reserves. (biomedcentral.com)
  • The chymotrypsin-like fold of the S1 peptidase family presents an ideal catalytic platform that enables high turnover, substrate selectivity, and various modes of regulation in a package readily combined with additional protein domains (7). (schoolbag.info)
  • This entry represents the NLPC/P60 domain, which is a primitive, papain-like peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core [ PMID: 19217401 ]. (ebi.ac.uk)
  • Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. (ebi.ac.uk)
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (ebi.ac.uk)
  • From sequence similarities, cysteine peptidases can be clustered into over 80 different families [ PMID: 11517925 ]. (ebi.ac.uk)
  • Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. (ebi.ac.uk)
  • Peptidases in clan CA are usually sensitive to the small molecule inhibitor E64, which is ineffective against peptidases from other clans of cysteine peptidases [ PMID: 7044372 ]. (ebi.ac.uk)
  • Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. (ebi.ac.uk)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (ebi.ac.uk)
  • Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases. (ebi.ac.uk)
  • Biochemical and structural analysis of the peptide-hydrolyzing enzymes of bacteria have revealed a large diversity of peptidases with different catalytic mechanisms. (biomedcentral.com)
  • The N-terminal domain of TPPII contains a serine peptidase site, with a classical catalytic triad of serine peptidases (Ser-449-His-264-Asp-44) [ 7 ]. (hindawi.com)
  • A seventh catalytic type of proteolytic enzymes, asparagine peptide lyase, was described in 2011. (wikipedia.org)
  • the Gla domain , two tandem copies of the EGF domain and a C-terminal trypsin -like peptidase domain which carries out the catalytic cleavage. (ipfs.io)
  • Calcium-dependent cysteine protease (calpain) is a novel vaccine candidate that has been studied in S. mansoni , S. japonicum , and protozoans including malaria, leishmania and trypanosomes. (biomedcentral.com)
  • Concomitantly, a calcium-dependent cysteine peptidase was detected in the parasite extract, the activity of which was repressed by pre-incubation of parasites with MDL28170. (fiocruz.br)
  • The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability. (pnas.org)
  • It uses a catalytic triad of Cysteine-Histidine-Asparagine in its active site to perform covalent proteolysis of its substrate. (wikipedia.org)
  • Asparagine endopeptidase is synthesized as an inactive zymogen. (wikipedia.org)
  • We show that the eponymous asparagine-specific endopeptidase activity is electrostatically generated by pH shift. (pnas.org)
  • Nucleophilicity of the catalytic serine is commonly dependent on a catalytic triad of aspartic acid, histidine, and serine-commonly referred to as a charge relay system (3). (schoolbag.info)
  • Cysteine proteinases perform multiple functions in seeds, including participation in remodelling polypeptides and recycling amino acids during maturation and germination. (biomedcentral.com)
  • Furthermore, there is limited information on the cysteine proteinase inhibitors which influence the activities of these proteinases. (biomedcentral.com)
  • While it is believed that the key biological function of the plant cysteine proteinase inhibitors (CPI) is to modulate the function of target proteinases in-vivo , to date, only a limited number of CPI have been tested with plant cysteine proteinases. (biomedcentral.com)
  • Cysteine protease inhibitors are available that can block the active site but no such inhibitor available yet that can be targeted to block the pro-mature domain interactions and prevent it activation. (frontiersin.org)
  • Cathepsin B is a lysosomal cysteine protease with both endopeptidase and dipeptidyl carboxypeptidase activities. (creativebiomart.net)
  • Cathepsin D can be an aspartic lysosomal endopeptidase within most mammalian cells. (antibodyassay.com)
  • Rhodesain is the major cysteine protease of T. brucei rhodesiense, the causative agent of African sleeping sickness. (creativebiomart.net)
  • Structural Basis of Murein Peptide Specificity of a gamma-D-Glutamyl-L-Diamino Acid Endopeptidase. (burnham.org)
  • Two cysteine proteinase (CP) and four cysteine proteinase inhibitor (CPI) gene sequences have been identified in coffee with significant expression during the maturation and germination of coffee grain. (biomedcentral.com)
  • QRT-PCR expression analysis of the four cysteine proteinase inhibitor genes in Robusta showed that CcCPI-1 is primarily expressed in developing and germinating grain and CcCPI-4 is very highly expressed during the late post germination period, as well as in mature, but not immature leaves. (biomedcentral.com)
  • Several cysteine proteinase and cysteine proteinase inhibitor genes with strong, relatively specific expression during coffee grain maturation and germination are presented. (biomedcentral.com)
  • 2006). The ubiquitin carboxyl-terminal hydrolase (UCH) catalytic core of the USPs is typically around 350 amino acids, but consists of six conserved boxes, interspersed by insertion sites for additional sequence that can confer diversity (Ye et al. (atlasgeneticsoncology.org)
  • This cleft contains the active site, which contains a catalytic diad that has been likened to the catalytic triad of chymotrypsin. (slideplayer.info)
  • Covalent catalysis is performed with an Asp-His-Cys triad, split between the two barrels (Asp on β1 and His and Cys on β2). (wikipedia.org)
  • Cruzain is the only parasitic cysteine protease with a crystal structure. (creativebiomart.net)
  • One subdomain consists of a bundle of helices, with the catalytic Cys at the end of one of them, and the other subdomain is a beta-barrel with the active site His and Asn (or Asp). (ebi.ac.uk)
  • The active site features a novel Cys-His-His catalytic triad that appears to be a unique structural signature of this cysteine peptidase family. (rostlab.org)
  • its prodomain confers its latency, and its catalytic domain has a zinc atom in its active site. (hindawi.com)
  • AEP and other cysteine peptidase are activated when pH changes from neutral to acidic. (wikipedia.org)
  • [5] TPP1 contains a globular structure with a subtilisin -like fold, a Ser 475- Glu 272- Asp 360 catalytic triad. (wikidoc.org)
  • 2009). The major insertion in USP15 is between boxes 3/4, and embeds an ubiquitin-like fold (UBL) domain within the catalytic domain. (atlasgeneticsoncology.org)
  • Aspartate-158 was thought to play a role analogous to the role of aspartate in the serine protease catalytic triad, but that has since then been disproved. (slideplayer.info)
  • This results in a partial detachment of the catalytic domain from the disk-like apple domains, still linked to the fourth domain with a disulfide bond, but now farther from the third domain. (wikidoc.org)
  • Endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme contains two major domains: a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. (ebi.ac.uk)
  • The crystal structures of two homologous endopeptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme were determined at 1.05 and 1.60 A resolution, respectively, and contain a bacterial SH3-like domain (SH3b) and a ubiquitous cell-wall-associated NlpC/P60 (or CHAP) cysteine peptidase domain. (scripps.edu)
  • The results of computational modeling, molecular dynamics simulations, and targeted amino acid mutagenesis indicate that the backbone amide of Glu(224) and the side chain of Arg(233) form an oxyanion hole in sortase B that stabilizes high energy tetrahedral catalytic intermediates. (anl.gov)
  • Twenty-three DE genes encoding trypsins, metalloproteinases, and serine-type endopeptidases were significantly upregulated in midguts of mosquitoes at day 1 following SM or PM ingestion. (biomedcentral.com)
  • The protease functions in the lysosome to cleave N-terminal tripeptides from substrates and has weaker endopeptidase activity. (wikidoc.org)
  • The original Christmas disease mutation was identified by sequencing of Christmas' DNA, revealing a mutation which changed a cysteine to a serine. (ipfs.io)
  • Molecular function: cysteine-type endopeptidase activity. (expasy.org)
  • Papain is a cysteine protease extracted from the tropical papaya fruit. (creativebiomart.net)
  • In 1937, papain was the first cysteine protease isolated and characterized from Carica papaya ( Walsh, 2014 ). (frontiersin.org)
  • The primarily endolysosomal cysteine protease legumain exemplifies how intricate multifactorial processes combine in zymogen activation and activity regulation ( 2 ⇓ - 4 ). (pnas.org)
  • By a pH-induced activation route, legumain was shown to develop asparaginyl-specific endopeptidase (AEP) activity that is used synonymously for the legumain ( 3 , 11 ). (pnas.org)
  • This catalytic activity is known as glutamine amidotransferase (GATase) (EC 2.4.2. (expasy.org)
  • [1] [2] Among other things it is heavily implicated in MHC (HLA) class-I processing, as it has both endopeptidase and exopeptidase activity. (wikidoc.org)
  • a href='/help/catalytic_activity' target='_top'>More. (uniprot.org)
  • Broad endopeptidase activity. (uniprot.org)
  • The proteasome activity can be complemented in the cytosol by endopeptidases ( Figure 1 ) [1] , [2] . (prolekare.cz)
  • It has been reported that NEP is modified by HNE and catalytic activity of HNE-modified NEP is decreased in AD brains and in HNE- or Aβ-treated cells [ 29 , 30 ]. (bioscirep.org)
  • This has allowed us to isolate for the first time a highly pure rhomboid with catalytic activity. (embopress.org)
  • suggest that the Tc24 is a B-cell superantigen based on the observations that 1) Tc24 was hydrolyzed by IgM present in serum of unexposed mice and human beings Salinomycin and 2) contact with Tc24 removed catalytic activity as soon as 4 times after infection. (welbourneprimary.com)
  • 2009). The intercalation of a UBL between boxes 3 and 4 of the catalytic domain increases the spacing between two sets of zinc-coordinating cysteine motifs, which form a functional zinc finger that is required for activity (Hetfeld et al. (atlasgeneticsoncology.org)
  • We designed, synthesized and characterized three novel polymeric Turn-ON probes that will be activated at the tumor site by cysteine cathepsins that are highly expressed in multiple tumor types. (thno.org)
  • TEV protease (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine protease from Tobacco Etch Virus (TEV). (wikipedia.org)
  • They exhibit low sequence conservation, but have high structural similarity with ubiquitin and have been proposed to play important roles in regulating DUB catalytic function or interactions (Zhu et al. (atlasgeneticsoncology.org)
  • The first approach focuses on decreasing the immunogenic content of gluten, using strategies like genetically modified wheat, intra-intestinal gluten digestion using glutenases, microwave thermal treatment of hydrated wheat kernels, and gluten pretreatment with either bacterial/ fungal derived endopeptidases or microbial transglutaminase. (frontiersin.org)
  • Here, we report the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde. (nih.gov)
  • This family includes the Escherichia coli membrane-associated lipoprotein N1pC, and possesses a catalytic domain containing a conserved amino-terminal cysteine and a carboxy-terminal histidine. (biomedcentral.com)
  • Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad. (rostlab.org)
  • The profile we developed covers the entire GATase type 1 domain, including the catalytic Cys in the N-terminal half of the domain and the conserved His and Glu of the triad in the C-terminal part of the domain. (expasy.org)
  • Both contain a collagen-binding domain within their catalytic domain, distinguishing them from other MMPs. (hindawi.com)
  • Factor XI consists of four apple domains , that create a disk-like platform around the base of a fifth, catalytic serine protease domain. (wikidoc.org)
  • Our predicted models from protozoa, archaea, fungi and plants were combined with the experimentally determined structures of 16 S1 family members and used for analysis of the catalytic core. (pubmedcentralcanada.ca)
  • Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. (wikipedia.org)
  • Matrix metalloproteinases (MMPs) are zinc-dependent endopeptidases that efficiently degrade the components of the ECM and basement membranes (BM). (hindawi.com)