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.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.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.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Thiorphan: A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.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.Protease Inhibitors: Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).Kinetics: The rate dynamics in chemical or physical systems.Cysteine Proteases: A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Cysteine Proteinase Inhibitors: Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.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.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.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.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.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.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.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.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)Dipeptides: Peptides composed of two amino acid units.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.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Serine Proteinase Inhibitors: Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.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.Oligopeptides: Peptides composed of between two and twelve amino acids.Aspartic Acid Endopeptidases: A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.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).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.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.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.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.Sulfhydryl Compounds: Compounds containing the -SH radical.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.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.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.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.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.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.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).Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.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.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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Bacterial Proteins: Proteins found in any species of bacterium.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
... and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec) Cathepsin V is a human lysosomal cysteine ... endopeptidase. Cathepsin L2 Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human cathepsin V functional expression, tissue ... Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine ...
Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... The next step is nucleophilic attack by the deprotonated cysteine's anionic sulfur on the substrate carbonyl carbon. In this ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ... Cysteine Peptidase. Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. Rendered ...
C-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the ... substrate protein, and may be any of several amino acids This enzyme belongs to the peptidase family M48. Tam, A.; Schmidt, W.K ... Ste24 endopeptidase (EC 3.4.24.84) is an enzyme. This enzyme catalyses the following chemical reaction The peptide bond ... Ste24 endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ...
It uses a catalytic triad of Cysteine-Histidine-Asparagine in its active site to perform covalent proteolysis of its substrate ... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Lett. 441: 361-365. doi:10.1016/S0014-5793(98)01574- ... Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). ... their C-terminal domain binds over their active site (where a substrate would normally bind), inhibiting activity. Once in the ...
This enzyme catalyses the following chemical reaction Preferential cleavage: Gly-, in proteins and small molecule substrates ... "Affinity purification of the novel cysteine proteinase papaya proteinase IV and papain from papaya latex". Biochem. J. 261: 469 ... Glycyl endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Molecular and Cellular Biology ... Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, chymopapain, Papaya ...
Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ... Promiscuous proteases typically bind to a single amino acid on the substrate and so only have specificity for that residue. For ... 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 ...
Shows weak endopeptidase activity Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). Nägler, D.K.; ... McDonald, J.K.; Ellis, S. (1975). "On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate ... Nägler, D.K.; Ménard, R. (1998). "Human cathepsin X: A novel cysteine protease of the papain family with a very short proregion ... Santamaría, I.; Velasco, G.; Pendás, A.M.; Fueyo, A.; López-Otín, C. (1998). "Cathepsin Z, a novel human cysteine proteinase ...
In humans, the group of cathepsin cysteine proteases or cysteine cathepsins comprises 11 family members, cathepsins B, C, F, H ... which provides the substrate specificity Small hinge region, which allows the hemopexin domain to bring the substrate to the ... MMPs are a large multigene family of zinc-dependent endopeptidases. The collective MMP family is capable of degrading all known ... All of these components of the basement membrane are substrates for MMP-2, 3, 7, and 9, among others. Inhibitors of MMP ...
... (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine ... Residues of the substrate are labelled P6 to P1 before the cut site and P1' after the cut site. Early works also measured ... Although ENLYFQ\S is the optimal sequence, the protease is active to a greater or lesser extent on a range of substrates (i.e. ... This tunnel contains a set of tight binding pockets such that each side chain of the substrate peptide (P6 to P1') is bound in ...
... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ... As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the ... By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that ...
... a conserved cysteine residue that interacts with the zinc in the active site and prevents binding and cleavage of the substrate ... They are distinguished from other endopeptidases by their dependence on metal ions as cofactors, their ability to degrade ... The "cysteine switch" was described in 1990. The MMPs have a common domain structure. The three common domains are the pro- ... The main substrates of the gelatinases are type IV collagen and gelatin, and these enzymes are distinguished by the presence of ...
"Identification of a novel maturation mechanism and restricted substrate specificity for the SspB cysteine protease of ... Glutamyl endopeptidase proteolytically activates the zymogen of the cysteine protease staphopain B (staphopain A is activated ... Glutamyl endopeptidase is in S. aureus expressed from the gene sspA within the operon ssp. Downstream of sspA, the operon also ... Glutamyl endopeptidase is expressed as a zymogen that, in order to become fully active, has been modified both through ...
This enzyme catalyses the following chemical reaction: Hydrolysis of proteins and small molecule substrates, with a preference ... arginine-specific cysteine protease, arginine-specific gingipain, arginine-specific gingivain, RGP-1, RGP) is an enzyme. ... a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase ... "Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis". J. Biol. Chem. ...
GPR endopeptidase family) Clan AF (e.g. Omptin family) Many eukaryotic aspartic endopeptidases (MEROPS peptidase family A1) are ... Unlike serine or cysteine proteases these proteases do not form a covalent intermediate during cleavage. Proteolysis therefore ... Rearrangement of this intermediate leads to protonation of the scissile amide which results in the splitting of the substrate ... Aspartic endopeptidases EC 3.4.23. of vertebrate, fungal and retroviral origin have been characterised. More recently, aspartic ...
The TIMP contact the catalytic cleft of the MMP in a similarly as a substrate. TIMPs inhibit all MMPs except TIMP-1 which does ... They all contain twelve cysteine residues that form six disulfide bonds. These bonds are critical for the conformation of the N ... MMPs belong to a family of zinc-dependent neutral endopeptidases. These enzymes have the ability to break down connective ... MMP activity can be decreased by binding to the cleavage site on the substrate e.g. catechin. Two molecular features of most ...
The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine endopeptidases at the US National ... The next step is nucleophilic attack by the deprotonated cysteine's anionic sulfur on the substrate carbonyl carbon. In this ... In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as ... Within each superfamily, families are designated by their catalytic nucleophile (C = cysteine proteases). Families of Cysteine ...
"Entry of ADAM10 endopeptidase (EC-Number 3.4.24.81 )". Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E ... The disintigrin and cysteine-rich domain (shown to the right) plays an essential role in regulation of protease activity in ... Although a single sheddase may "shed" a variety of substances, multiple sheddases can cleave the same substrate resulting in ... Smith KM, Gaultier A, Cousin H, Alfandari D, White JM, DeSimone DW (December 2002). "The cysteine-rich domain regulates ADAM ...
For example, SMEP1 is said to have a free cysteine at position 94, a non-homologous insert from V103 to S121, a free sulfhydryl ... Cao, J. & Zucker, S. (n.d.). Introduction to the MMP and TIMP families (structures, substrates) and an overview of diseases ... Matrix metalloproteinases (MMPs) are zinc endopeptidases, commonly called metzincins. MMP enzymes represent an ancient family ... Plant MMPs show structural similarity to MMPs found in mammals, such as the presence of an auto-regulatory cysteine switch ...
... 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 ... "Defining the substrate specificity of mouse cathepsin P". Archives of Biochemistry and Biophysics. 435 (1): 190-6. doi:10.1016/ ... "Entrez Gene: CTSZ cathepsin Z". Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, Turk D (January 2012). "Cysteine ...
The model proposed by Mozingo and Robertus, based on X-ray structures, is as follows: Sarcin-ricin loop substrate binds RTA ... The propolypeptide is cleaved within protein bodies by an endopeptidase to produce the mature ricin protein that is composed of ... ER the propolypeptide is glycosylated and a protein disulfide isomerase catalyzes disulfide bond formation between cysteines ... In particular, Arg180 and Glu177 have been shown to be involved in the catalytic mechanism, and not substrate binding, with ...
... yeast cysteine proteinase E. Now EC 3.4.25.1, proteasome endopeptidase complex EC 3.4.22.22: Transferred entry: yeast cysteine ... tissue endopeptidase degrading collagenase synthetic substrate. Now EC 3.4.24.15, thimet oligopeptidase EC 3.4.99.32: ... Ste24 endopeptidase EC 3.4.24.85: S2P endopeptidase EC 3.4.24.86: ADAM 17 endopeptidase EC 3.4.24.87: ADAMTS13 endopeptidase EC ... ADAM10 endopeptidase EC 3.4.24.82: ADAMTS-4 endopeptidase EC 3.4.24.83: anthrax lethal factor endopeptidase EC 3.4.24.84: ...
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 forms an alpha-helical domain that runs through the substrate-binding site, preventing access. Removal of this region by ... It has no similarity to any other known cysteine proteinase inhibitors but bears some similarity to a lectin-like family of ...
... deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase". Biol. Chem. 384 (9): 1327-32. ... Pol E, Björk I (2001). "Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition ... The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins ... Fuchs R, Gassen HG (1990). "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase". Nucleic Acids Res ...
"Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants". The Journal of ... 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) ...
Cathepsin K is a collagenolytic, papain-like, cysteine protease that is mainly expressed in osteoclasts, and is secreted into ... The matrix metalloproteinases (MMPs) comprise a family of more than 20 zinc-dependent endopeptidases. The role of matrix ... major osteoclast proteins but have significant differences from cells in living bone because of the not-natural substrate. The ... The function of these cysteine and aspartic proteases is generally unknown within bone, and they are expressed at much lower ...
Some of the substrate-bound conformations bear high similarity to the substrate-free ones, but they are not entirely identical ... This is then transferred to E1's active-site cysteine residue in concert with the adenylylation of a second ubiquitin.[48] This ... Wilk S, Orlowski M (November 1980). "Cation-sensitive neutral endopeptidase: isolation and specificity of the bovine pituitary ... indicating that energy from ATP hydrolysis is used for substrate unfolding.[27] Passage of the unfolded substrate through the ...
As neprilysin has a broad substrate specificity and is localized subcellularly in the vicinity of PrP, it represents a ... As neprilysin has a broad substrate specificity and is localized subcellularly in the vicinity of PrP, it represents a ... Scrapie protein degradation by cysteine proteases in CD11c+ dendritic cells and GT1-1 neuronal cells. J Virol 78, 4776-4782.[ ... Neutral endopeptidase modulation of septic shock. J Exp Med 181, 2271-2275.[CrossRef] ...
Proteases such as calpain-1 (Yamazaki et al., 1997), furin (Pearton et al., 2001), PEP1 (profilaggrin endopeptidase 1; Resing ... Proprotein convertase expression and localization in epidermis: evidence for multiple roles and substrates. Exp. Dermatol. ... a cysteine protease that reversibly disrupts TJs (Wan et al., 1999). Apparently, Derp1 acts to increase paracellular ... Proprotein convertase expression and localization in epidermis: evidence for multiple roles and substrates. Exp. Dermatol. ...
latex displaying high substrate specificity. Together they form a unique fingerprint. * Vasconcellea quercifolia Agriculture ... Fingerprint Dive into the research topics of Purification and characterization of a cysteine endopeptidase from vasconcellea ... Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. latex displaying high ... Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. latex displaying high ...
Asparaginyl endopeptidase (AEP or legumain) is a lysosomal cysteine protease that cleaves protein substrates on the C-terminal ... Asparaginyl endopeptidase (AEP or legumain) is a lysosomal cysteine protease that cleaves protein substrates on the C-terminal ... Mice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome. Chi-Bun Chan, Michiyo Abe, ... Mice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome. Chi-Bun Chan, Michiyo Abe, ...
Purification and Characterization of a Cysteine Endopeptidase from Vasconcellea quercifolia A. St.-Hil. Latex Displaying High ... Substrate Specificity Article Title:. Journal of agricultural and food chemistry.. Author:. Torres, M. Jose. View in NALs ... 5. Cloning, site-directed mutagenesis and expression of cathepsin L-like cysteine protease from Uronema marinum (Ciliophora: ...
... cleave peptides proximal to the amino or carboxy termini of the substrate; endopeptidases (serine, aspartic, cysteine and ... After evaluating many fluorescent substrates, we chose assay substrates for cysteine proteases (papain) and serine proteases ( ... Cleavage of the cysteine protease substrate results in fluorescence at 460nm, and cleavage of the serine protease results in ... A quenched-fluorescent substrate with pancreatic tissue extract was used and fluorescence measured after substrate cleavage. ...
The most abundant of the cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus. Distinct from the ... Broad specificity for cleavage of proteins, but strong preference for Z-Arg-Arg!NHMec amongst small molecule substrates. ...
Cysteine endopeptidases. Reaction(IUBMB). Broad proteolytic activity. With small-molecule substrates and inhibitors, the major ... Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin ... Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. ... Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification. ...
Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... The next step is nucleophilic attack by the deprotonated cysteines anionic sulfur on the substrate carbonyl carbon. In this ... The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases. *Cysteine+endopeptidases at the US ... Cysteine Peptidase. Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. Rendered ...
Involved in cysteine-type endopeptidase activity. Specific function:. Mediates GPI anchoring in the endoplasmic reticulum, by ... During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Gene Name: ... 3-linkage to some substrate. Glycolipids probably serve for adherence of some pathogens. Gene Name:. GBGT1. Uniprot ID:. Q8N5D6 ...
Involved in cysteine-type endopeptidase activity. Specific function:. Mediates GPI anchoring in the endoplasmic reticulum, by ... SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values. Gene Name:. ST3GAL1. Uniprot ID:. ... During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein. Gene Name: ... Has sialidase activity towards synthetic substrates, such as 2-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (4-MU- ...
... and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec) Cathepsin V is a human lysosomal cysteine ... endopeptidase. Cathepsin L2 Brömme, D.; Li, Z.; Barnes, M.; Mehler, E. (1999). "Human cathepsin V functional expression, tissue ... Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. (1998). "Cathepsin L2, a novel human cysteine ...
... is a secreted cysteine endopeptidase from the human pathogen S. pyogenes with an extraordinarily high degree of substrate ... Structure of the streptococcal endopeptidase IdeS, a cysteine proteinase with strict specificity for IgG. Wenig, K., Chatwell, ... Anatomical context of Substrate Specificity. *The strict substrate specificity of this reaction suggests that L-arginine is the ... Gene context of Substrate Specificity. *The substrate specificity of the truncated RAD2 protein implicates branched DNA ...
... a cysteine endopeptidase of unusual substrate specificity.. Biochemistry. , 34(40), 13190-13195. ... Mansur F, Luoga W, Buttle DJ, Duce IR, Lowe AE & Behnke JM (2016) The anthelmintic efficacy of natural plant cysteine ... Mansur F, Luoga W, Buttle DJ, Duce IR, Lowe A & Behnke JM (2015) The anthelmintic efficacy of natural plant cysteine ... Mansur F, Luoga W, Buttle DJ, Duce IR, Lowe A & Behnke JM (2015) The anthelmintic efficacy of natural plant cysteine ...
Cysteine endopeptidase assay.Cysteine protease activity present in ammonium sulfate-precipitated culture supernatants was ... The cleavage of substrate and generation of product were determined to be linear with time to an A405 of 1.5. The cysteine ... Cleavage of the substrate was monitored by measuring the A405 over time in a microtiter plate reader (Biotek, Winooska, Vt.). ... Following incubation for 30 min at 37°C to allow reduction, 150 μl of the substrate-buffer solution (3.2 ml of 2.5 mM Bz-Pro- ...
Plants encode a unique group of papain-type cysteine endopeptidases (CysEP) characterized by a C-terminal KDEL endoplasmic ... In concordance with previous studies, showing that ABA DEFICIENT3 uses Cys as the substrate for activation of the ABSCISIC ... The role of KDEL-tailed cysteine endopeptidases of Arabidopsis (AtCEP2 and AtCEP1) in root development ... Sulfate is Incorporated into Cysteine to Trigger ABA Production and Stomatal Closure ...
... have a cysteine residue in their active side and therefore employ the sulfhydryl group of the side chain of a cysteine residue ... 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 ... Clan CD Cysteine Proteases. Clan CD is a smaller class of cysteine proteases compared to clan CA cysteine proteases. ...
In addition, these enzymes all have γ-d-Glu-A 2pm (A 2pm is diaminopimelic acid) cysteine amidase (ordl-endopeptidase) ... To avoid cleavage of unintended substrates, these enzymes have very selective substrate specificities. Our biochemical and ... remodel the substrate binding site, and modulate substrate specificity. Two amino acid differences at the domain interface ... Title: Insights into substrate specificity of NlpC/P60 cell wall hydrolases containing bacterial SH3 domains ...
Cysteine Endopeptidases / chemistry* * Cysteine Endopeptidases / genetics * Cysteine Endopeptidases / metabolism* * Cytokines ... We show that PLpro greatly prefers K48- to K63-linked ubiquitin chains, and ISG15-based substrates to those that are mono- ... However, a select number of these mutants have a significantly reduced ability to hydrolyze the substrate ISG15-AMC, or be ... of PLpro in complex with ubiquitin-aldehyde and model the interaction of PLpro with other ubiquitin-chain and ISG15 substrates ...
Cysteine Proteinase Inhibitors (30) • Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES. MeSH ... especially in the form of enzyme substrates. Synonym: chromogens (not to be confused with pigment-synthesizing bacteria also ... Cysteine Proteinase Inhibitors, Endogenous (0) see Cysteine Proteinase Inhibitors. Cysteine Proteinase Inhibitors, Exogenous (0 ... see Cysteine Proteinase Inhibitors. Cystine Depleting Agents (1) • Compounds and drugs that react with CYSTINE and convert it ...
Cysteine Endopeptidases/*metabolism, Enzyme Inhibitors/pharmacology, Epithelium/drug effects/enzymology, Human, Ionomycin/ ... RESULTS: After administration of substrate to the medium overlying the cells, the substrate was degraded at a relatively slow ... The sample, with the cell-permeable substrate Suc-Leu-Leu-Val-Tyr-7-amino-4-methylcoumarin, was placed in a chamber, which was ... Proteolysis in human lens epithelium determined by a cell-permeable substrate. Artikel i vetenskaplig tidskrift ...
Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity.,OHara ... Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity. ... Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to ... Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently bound to the catalytic Cys ...
Å crystal structure amd substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell death of ... Schmid M, Simpson D, Kalousek F, Gietl C (1998) A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean ... Gietl C, Wimmer B, Adamec J, Kalousek F (1997) A cysteine endopeptidase isolated from castor bean endosperm microbodies ... 10 μl AtDEG15 (Ni-TED column eluate) were incubated with ten μl substrate (pre-gMDH, pre-gCS or pre-thiolase) in the presence ( ...
Aside from previously known general catabolic functions and protein processing, cysteine proteases may be key to parasite ... Cysteine proteases play numerous indispensable roles in the biology of parasitic organisms. ... diverse substrate specificity and cellular location. The disparate nature of parasite cysteine protease compared to the host ... and the newly discovered class of asparaginyl-endopeptidases. Cysteine protease classification will be re-examined in light of ...
The 2.0 Å crystal structure amd substrate specificity of the KDEL-tailed cysteine endopeptidase functioning in programmed cell ... A cysteine endopeptidase with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinosome ... A cysteine endopeptidase isolated from castor bean endosperm microbodies processes the glyoxysomal malte dehydrogenase ... which is accompanied by a change in substrate specificity from a general protease (monomer) to the specific cleavage of the ...
  • abstract = "A new proteolytic preparation from Vasconcellea quercifolia ({"}oak leaved papaya{"}) latex containing several cysteine endopeptidases with high proteolytic activity has been obtained. (uab.cat)
  • We present the X-ray crystal structure of PLpro in complex with ubiquitin-aldehyde and model the interaction of PLpro with other ubiquitin-chain and ISG15 substrates. (nih.gov)
  • We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. (nih.gov)
  • We have studied the effects of IFN-gamma-independent LMP incorporation on the quality of peptides processed from the murine cytomegalovirus IE pp89 25-mer polypeptide substrate through dual cleavages by 20S proteasomes. (mdc-berlin.de)
  • There exists, however, no obvious correlation between the observed changes in hydrolytic activities against short fluorogenic peptides and the changes in dual cleavage site usage within the 25-mer polypeptide substrate. (mdc-berlin.de)
  • Bleomycin hydrolase acts mainly as an aminopeptidase on short peptides, but the rat orthologue has been shown to cleave amyloid beta-peptides, acting as an endopeptidase or a carboxypeptidase, as well as an aminopeptidase [ PMID: 16472072 ]. (ebi.ac.uk)
  • 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)
  • Here we report the crystal structure of a Methanococcus maripaludis homologue of Rce1, whose endopeptidase specificity for farnesylated peptides mimics that of eukaryotic Rce1. (sigmaaldrich.com)
  • We show that the eponymous asparagine-specific endopeptidase activity is electrostatically generated by pH shift. (pnas.org)
  • When the several hydrolytic activities are tested with short fluorogenic peptide substrates, the Vmax, S0.5 (Km), or both values of 20S proteasomes are altered, depending on the combination of LMP. (mdc-berlin.de)
  • This current work presents kinetic studies of recombinant bromelain (recBM) expressed in Escherichia coli BL21-AI on four synthetic substrates, N-α-carbobenzoxy-L-alanyl-p-nitrophenyl ester (ZANPE), N-α-carbobenzoxy-L-arginyl-L-arginine-p-nitroanilide (ZAANA), N-α-carbobenzoxy-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide (ZPVANA) and L-pyroglutamyl-L-phenylalanyl-L-leucine-p-nitroanilide (PFLNA). (scirp.org)