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.
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 thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
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 multiprotein complex composed of the products of c-jun and c-fos proto-oncogenes. These proteins must dimerize in order to bind to the AP-1 recognition site, also known as the TPA-responsive element (TRE). AP-1 controls both basal and inducible transcription of several genes.
Cellular DNA-binding proteins encoded by the c-jun genes (GENES, JUN). They are involved in growth-related transcriptional control. There appear to be three distinct functions: dimerization (with c-fos), DNA-binding, and transcriptional activation. Oncogenic transformation can take place by constitutive expression of c-jun.
An IRON-containing protein that uses siroheme and 4Fe-4S iron-sulfur centers as prosthetic groups. It catalyzes the six-electron oxidation of AMMONIA to nitrite.
Eighteen-carbon cyclopentyl polyunsaturated fatty acids derived from ALPHA-LINOLENIC ACID via an oxidative pathway analogous to the EICOSANOIDS in animals. Biosynthesis is inhibited by SALICYLATES. A key member, jasmonic acid of PLANTS, plays a similar role to ARACHIDONIC ACID in animals.
A group of alicyclic hydrocarbons with the general formula R-C5H9.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
A group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 1.
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
A protease of broad specificity, obtained from dried pancreas. Molecular weight is approximately 25,000. The enzyme breaks down elastin, the specific protein of elastic fibers, and digests other proteins such as fibrin, hemoglobin, and albumin. EC 3.4.21.36.
An enzyme that catalyzes the hydrolysis of proteins, including elastin. It cleaves preferentially bonds at the carboxyl side of Ala and Val, with greater specificity for Ala. EC 3.4.21.37.
Large, transmembrane, non-covalently linked glycoproteins (alpha and beta). Both chains can be polymorphic although there is more structural variation in the beta chains. The class II antigens in humans are called HLA-D ANTIGENS and are coded by a gene on chromosome 6. In mice, two genes named IA and IE on chromosome 17 code for the H-2 antigens. The antigens are found on B-lymphocytes, macrophages, epidermal cells, and sperm and are thought to mediate the competence of and cellular cooperation in the immune response. The term IA antigens used to refer only to the proteins encoded by the IA genes in the mouse, but is now used as a generic term for any class II histocompatibility antigen.
The process by which antigen is presented to lymphocytes in a form they can recognize. This is performed by antigen presenting cells (APCs). Some antigens require processing before they can be recognized. Antigen processing consists of ingestion and partial digestion of the antigen by the APC, followed by presentation of fragments on the cell surface. (From Rosen et al., Dictionary of Immunology, 1989)
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Membrane antigens associated with maturation stages of B-lymphocytes, often expressed in tumors of B-cell origin.
A psychoactive compound extracted from the resin of Cannabis sativa (marihuana, hashish). The isomer delta-9-tetrahydrocannabinol (THC) is considered the most active form, producing characteristic mood and perceptual changes associated with this compound.
The plant genus in the Cannabaceae plant family, Urticales order, Hamamelidae subclass. The flowering tops are called many slang terms including pot, marijuana, hashish, bhang, and ganja. The stem is an important source of hemp fiber.
A subclass of cannabinoid receptor found primarily on central and peripheral NEURONS where it may play a role modulating NEUROTRANSMITTER release.
Compounds having the cannabinoid structure. They were originally extracted from Cannabis sativa L. The most pharmacologically active constituents are TETRAHYDROCANNABINOL; CANNABINOL; and CANNABIDIOL.
Inhaling and exhaling the smoke from CANNABIS.
A class of G-protein-coupled receptors that are specific for CANNABINOIDS such as those derived from CANNABIS. They also bind a structurally distinct class of endogenous factors referred to as ENDOCANNABINOIDS. The receptor class may play a role in modulating the release of signaling molecules such as NEUROTRANSMITTERS and CYTOKINES.
Compound isolated from Cannabis sativa extract.
A plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida.
A plant genus of the family Caricaceae, order Violales, subclass Dilleniidae, class Magnoliopsida. It is the source of edible fruit and PAPAIN.
A milky, product excreted from the latex canals of a variety of plant species that contain cauotchouc. Latex is composed of 25-35% caoutchouc, 60-75% water, 2% protein, 2% resin, 1.5% sugar & 1% ash. RUBBER is made by the removal of water from latex.(From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed). Hevein proteins are responsible for LATEX HYPERSENSITIVITY. Latexes are used as inert vehicles to carry antibodies or antigens in LATEX FIXATION TESTS.
A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.
A proposed family of bacteria belonging to the alpha-2 subgroup of PROTEOBACTERIA.
A genus of gram-negative, rod-shaped, phototrophic bacteria found in aquatic environments. Internal photosynthetic membranes are present as lamellae underlying the cytoplasmic membrane.
Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.
A class in the phylum PROTEOBACTERIA comprised mostly of two major phenotypes: purple non-sulfur bacteria and aerobic bacteriochlorophyll-containing bacteria.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
A phylum of parasitic worms, closely related to tapeworms and containing two genera: Moniliformis, which sometimes infects man, and Macracanthorhynchus, which infects swine.
A genus of nematode intestinal parasites that consists of several species. A. duodenale is the common hookworm in humans. A. braziliense, A. ceylonicum, and A. caninum occur primarily in cats and dogs, but all have been known to occur in humans.
A superfamily of parasitic nematodes which were formerly considered a part of TRICHOSTRONGYLOIDEA. It includes the following genera: Heligmosomum, NEMATOSPIROIDES, and NIPPOSTRONGYLUS. The hosts are rodents.
Infection of humans or animals with hookworms of the genus ANCYLOSTOMA. Characteristics include anemia, dyspepsia, eosinophilia, and abdominal swelling.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
Protein-digesting and milk-clotting enzymes found in PINEAPPLE fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. This enzyme was formerly listed as EC 3.4.22.4.
A parasite of carnivorous mammals that causes TRICHINELLOSIS. It is especially common in rats and in swine fed uncooked garbage. Human infection is initiated by the consumption of raw or insufficiently cooked pork or other meat containing the encysted larvae.
A family (Aphididae) of small insects, in the suborder Sternorrhyncha, that suck the juices of plants. Important genera include Schizaphis and Myzus. The latter is known to carry more than 100 virus diseases between plants.
A large genus of plant viruses of the family POTYVIRIDAE which infect mainly plants of the Solanaceae. Transmission is primarily by aphids in a non-persistent manner. The type species is potato virus Y.
The simplest of all peptides. It functions as a gamma-glutamyl acceptor.
The type species of AQUABIRNAVIRUS, causing infectious pancreatic necrosis in salmonid fish and other freshwater and marine animals including mollusks.
Peptides composed of two amino acid units.
Proteins that bind to RNA molecules. Included here are RIBONUCLEOPROTEINS and other proteins whose function is to bind specifically to RNA.

Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. (1/6256)

The lysosomal cysteine proteases cathepsins S and L play crucial roles in the degradation of the invariant chain during maturation of MHC class II molecules and antigen processing. The p41 form of the invariant chain includes a fragment which specifically inhibits cathepsin L but not S. The crystal structure of the p41 fragment, a homologue of the thyroglobulin type-1 domains, has been determined at 2.0 A resolution in complex with cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The first subdomain is an alpha-helix-beta-strand arrangement, whereas the second subdomain has a predominantly beta-strand arrangement. The wedge shape and three-loop arrangement of the p41 fragment bound to the active site cleft of cathepsin L are reminiscent of the inhibitory edge of cystatins, thus demonstrating the first example of convergent evolution observed in cysteine protease inhibitors. However, the different fold of the p41 fragment results in additional contacts with the top of the R-domain of the enzymes, which defines the specificity-determining S2 and S1' substrate-binding sites. This enables inhibitors based on the thyroglobulin type-1 domain fold, in contrast to the rather non-selective cystatins, to exhibit specificity for their target enzymes.  (+info)

C/EBPalpha regulates generation of C/EBPbeta isoforms through activation of specific proteolytic cleavage. (2/6256)

C/EBPalpha and C/EBPbeta are intronless genes that can produce several N-terminally truncated isoforms through the process of alternative translation initiation at downstream AUG codons. C/EBPbeta has been reported to produce four isoforms: full-length 38-kDa C/EBPbeta, 35-kDa LAP (liver-enriched transcriptional activator protein), 21-kDa LIP (liver-enriched transcriptional inhibitory protein), and a 14-kDa isoform. In this report, we investigated the mechanisms by which C/EBPbeta isoforms are generated in the liver and in cultured cells. Using an in vitro translation system, we found that LIP can be generated by two mechanisms: alternative translation and a novel mechanism-specific proteolytic cleavage of full-length C/EBPbeta. Studies of mice in which the C/EBPalpha gene had been deleted (C/EBPalpha-/-) showed that the regulation of C/EBPbeta proteolysis is dependent on C/EBPalpha. The induction of C/EBPalpha in cultured cells leads to induced cleavage of C/EBPbeta to generate the LIP isoform. We characterized the cleavage activity in mouse liver extracts and found that the proteolytic cleavage activity is specific to prenatal and newborn livers, is sensitive to chymostatin, and is completely abolished in C/EBPalpha-/- animals. The lack of cleavage activity in the livers of C/EBPalpha-/- mice correlates with the decreased levels of LIP in the livers of these animals. Analysis of LIP production during liver regeneration showed that, in this system, the transient induction of LIP is dependent on the third AUG codon and most likely involves translational control. We propose that there are two mechanisms by which C/EBPbeta isoforms might be generated in the liver and in cultured cells: one that is determined by translation and a second that involves C/EBPalpha-dependent, specific proteolytic cleavage of full-length C/EBPbeta. The latter mechanism implicates C/EBPalpha in the regulation of posttranslational generation of the dominant negative C/EBPbeta isoform, LIP.  (+info)

An antiviral mechanism of nitric oxide: inhibition of a viral protease. (3/6256)

Although nitric oxide (NO) kills or inhibits the replication of a variety of intracellular pathogens, the antimicrobial mechanisms of NO are unknown. Here, we identify a viral protease as a target of NO. The life cycle of many viruses depends upon viral proteases that cleave viral polyproteins into individual polypeptides. NO inactivates the Coxsackievirus protease 3C, an enzyme necessary for the replication of Coxsackievirus. NO S-nitrosylates the cysteine residue in the active site of protease 3C, inhibiting protease activity and interrupting the viral life cycle. Substituting a serine residue for the active site cysteine renders protease 3C resistant to NO inhibition. Since cysteine proteases are critical for virulence or replication of many viruses, bacteria, and parasites, S-nitrosylation of pathogen cysteine proteases may be a general mechanism of antimicrobial host defenses.  (+info)

Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. (4/6256)

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.  (+info)

Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. (5/6256)

The role of conformation-based quality control in the early secretory pathway is to eliminate misfolded polypeptides and unassembled multimeric protein complexes from the endoplasmic reticulum, ensuring the deployment of only functional molecules to distal sites. The intracellular fate of terminally misfolded human alpha1-antitrypsin was examined in hepatoma cells to identify the functional role of asparagine-linked oligosaccharide modification in the selection of glycoproteins for degradation by the cytosolic proteasome. Proteasomal degradation required physical interaction with the molecular chaperone calnexin. Altered sedimentation of intracellular complexes following treatment with the specific proteasome inhibitor lactacystin, and in combination with mannosidase inhibition, revealed that the removal of mannose from attached oligosaccharides abrogates the release of misfolded alpha1-antitrypsin from calnexin prior to proteasomal degradation. Intracellular turnover was arrested with kifunensine, implicating the participation of endoplasmic reticulum mannosidase I in the disposal process. Accelerated degradation occurred in a mannosidase-independent manner and was arrested by lactacystin, in response to the posttranslational inhibition of glucosidase II, demonstrating that the attenuated removal of glucose from attached oligosaccharides functions as the underlying rate-limiting step in the proteasome-mediated pathway. A model is proposed in which the removal of mannose from multiple attached oligosaccharides directs calnexin in the selection of misfolded alpha1-antitrypsin for degradation by the proteasome.  (+info)

Possible involvement of proteasomes (prosomes) in AUUUA-mediated mRNA decay. (6/6256)

We have identified a cellular target for proteasomal endonuclease activity. Thus, 20 S proteasomes interact with the 3'-untranslated region of certain cytoplasmic mRNAs in vivo, and 20 S proteasomes isolated from Friend leukemia virus-infected mouse spleen cells were found to be associated with a mRNA fragment showing great homology to the 3'-untranslated region of tumor necrosis factor-beta mRNA that contains AUUUA sequences. We furthermore demonstrate that 20 S proteasomes destabilize oligoribonucleotides corresponding to the 3'-untranslated region of tumor necrosis factor-alpha, creating a specific cleavage pattern. The cleavage reaction is accelerated with increasing number of AUUUA motifs, and major cleavage sites are localized at the 5' side of the A residues. These results strongly suggest that 20 S proteasomes could be involved in the destabilization of cytokine mRNAs such as tumor necrosis factor mRNAs and other short-lived mRNAs containing AUUUA sequences.  (+info)

Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia. (7/6256)

The formation of a persistently active cAMP-dependent protein kinase (PKA) is critical for establishing long-term synaptic facilitation (LTF) in Aplysia. The injection of bovine catalytic (C) subunits into sensory neurons is sufficient to produce protein synthesis-dependent LTF. Early in the LTF induced by serotonin (5-HT), an autonomous PKA is generated through the ubiquitin-proteasome-mediated proteolysis of regulatory (R) subunits. The degradation of R occurs during an early time window and appears to be a key function of proteasomes in LTF. Lactacystin, a specific proteasome inhibitor, blocks the facilitation induced by 5-HT, and this block is rescued by injecting C subunits. R is degraded through an allosteric mechanism requiring an elevation of cAMP coincident with the induction of a ubiquitin carboxy-terminal hydrolase.  (+info)

Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance. (8/6256)

PML/RARalpha is the leukemogenetic protein of acute promyelocytic leukemia (APL). Treatment with retinoic acid (RA) induces degradation of PML/RARalpha, differentiation of leukaemic blasts, and disease remission. However, RA resistance arises during RA treatment of APL patients. To investigate the phenomenon of RA resistance in APL, we generated RA-resistant sublines from APL-derived NB4 cells. The NB4.007/6 RA-resistant subline does not express the PML/RARalpha protein, although its mRNA is detectable at levels comparable to those of the parental cell line. In vitro degradation assays showed that the half-life of PML/RARalpha is less than 30 minutes in NB4.007/6 and longer than 3 hours in NB4. Treatment of NB4.007/6 cells with the proteasome inhibitors LLnL and lactacystin partially restored PML/RARalpha protein expression and resulted in a partial release of the RA-resistant phenotype. Similarly, forced expression of PML/RARalpha, but not RARalpha, into the NB4/007.6 cells restored sensitivity to RA treatment to levels comparable to those of the NB4 cells. These results indicate that constitutive degradation of PML/RARalpha protein may lead to RA resistance and that PML/RARalpha expression is crucial to convey RA sensitivity to APL cells.  (+info)

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2. Leu and Gln were most favoured at P2 and P1 positions, respectively. Substrate preferences at P5 to P3 positions were important in enhancing the main protease activity. Super-reactive substrate sequences were engineered, with more than a 2-fold increase in activity, by combining the best residue choices at P5 to P3 positions ...
Cell growth and viability are dependent on the function of the multicatalytic proteinase complex (proteasome), a multisubunit particle that affects progression through the mitotic cycle by degradation of cyclins. Exposure of rodent fibroblasts and human lymphoblasts in culture to benzyloxycarbonyl-leucyl-leucyl-phenylalaninal (Z-LLF-CHO), a cell-permeable peptidyl aldehyde inhibitor of the chymotrypsin-like activity of the proteasome, resulted in the induction of apoptosis in a rapid, dose-dependent fashion. Fibroblasts transformed with ras and myc, lymphoblasts transformed by c-myc alone, and a Burkitts lymphoma (BL) cell line that overexpresses c-Myc were up to 40-fold more susceptible to apoptosis than were either primary rodent fibroblasts or immortalized nontransformed human lymphoblasts, respectively. To determine whether such preferential apoptosis could impact upon tumor growth in vivo, toxicological studies were performed in mice with severe combined immunodeficiency and showed that ...
The SCOP classification for the CNF1/YfiH-like putative cysteine hydrolases superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
The SCOP classification for the CNF1/YfiH-like putative cysteine hydrolases superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
The beta coronavirus genome encodes several structural proteins, including the glycosylated spike(S) protein that functions as a major inducer of host immune responses. This S protein mediate shost cell invasion by SARS-CoV-2 via binding to a receptor protein called angiotensin-convertingenzyme 2 (ACE2) located on the surface membrane of host cells. A recent study also revealed that this invasion process requires S protein priming which is facilitated by the host cell-produced serine protease TMPRSS211. In addition, the viral genome also encodes several nonstructural proteins including RNA-dependent RNA polymerase (RdRp), coronavirus main protease (3CLpro), and papain-like protease (PLpro). Upon entrance to the host cells, the viral genome is released as a single-stranded positive RNA. Subsequently, it is translated into viral polyproteins using host cell proteintranslation machinery, which are then cleaved into effector proteins by viral proteinases 3CLpro and PLpro. PLpro also behaves as a ...
The AP-1 (activator protein-1) complex, which consists of proteins of the Fos and Jun families, is thought to play an important role in the balance between cell proliferation and apoptosis, the response to genotoxic stress ...
This 2018 JCI Insight paper by ZH Wang, etc utilizes the following products and services from Vector Biolabs: AAV-Cre-GFP (AAV serotype 6) AAV, AAV-GFP (AAV serotype 6) AAV.
Proteases are one of the largest and best-characterized families of enzymes in the human proteome. Unfortunately, the understanding of protease function in the context of complex proteolytic cascades remains in its infancy. One major reason for this gap in understanding is the lack of technologies t …
The picornaviral 3C protease mediates viral polyprotein maturation and multiple cleavages of host proteins to modulate viral translation and transcription. The 3C protease has been regarded as a valid target due to its structural similarity among different picornaviruses and minimal sequence similarity with host proteins; therefore, the development of potent inhibitors against the 3C protease as an antiviral drug is ongoing. Duck hepatitis A virus (DHAV) belongs to the Picornavidea family and is a major threat to the poultry industry. To date, little is known about the roles of the DHAV 3C protease plays during infection. In this study, we compared the full-length DHAV 3C protein sequence with other 3C sequences to obtain an alignment for the construction of a phylogenetic tree. Then, we expressed and purified recombinant DHAV 3C protease in the BL21 expression system using nickel-NTA affinity chromatography. The optimization of the cleavage assay conditions and the kinetic analysis for DHAV 3C protease
TY - JOUR. T1 - Characterization of legumain. AU - Schwarz, Gerold. AU - Brandenburg, Jens. AU - Reich, Michael. AU - Burster, Timo. AU - Driessen, Christoph. AU - Kalbacher, Hubert. PY - 2002/11. Y1 - 2002/11. N2 - The mammalian legumain, also called asparaginyl endopeptidase (AEP), is critically involved in the processing of bacterial antigens for MHC class II presentation. In order to investigate the substrate specificity of AEP in the P1 position, we created a peptide library and digested it with purified pig kidney AEP. Digestion was less efficient only when proline was in the P1 position. Maximum AEP activity was found in lysosomal fractions of different types of antigen presenting cells (APC). When the multiple sclerosis-associated autoantigen myelin basic protein (MBP) was digested with AEP, the immunodominant epitope 83-99 was destroyed. Myoglobin as an alternative substrate was AEP resistant. These results suggest an important, but not necessarily critical role for AEP in lysosomal ...
TY - JOUR. T1 - Expression of sweet potato asparaginyl endopeptidase caused altered phenotypic characteristics in transgenic Arabidopsis. AU - Chen, Hsien Jung. AU - Wen, I. Chia. AU - Huang, Guan Jhong. AU - Hou, Wen Chi. AU - Lin, Yaw Huei. PY - 2008/4. Y1 - 2008/4. N2 - We have previously isolated an asparaginyl endopeptidase, SPAE, from senescent leaves of sweet potato (Ipomoea batatas cv. Tainong 57). Gene expression of SPAE was activated and enhanced in natural and induced senescent leaves (Chen et al., 2004). In this report the full-length SPAE cDNA was constructed in the T-DNA portion of recombinant pBI121 vector under the control of CaMV 35S promoter and transferred to Arabidopsis with Agrobacterium-mediated floral dip transformation. Three transgenic Arabidopsis plants were isolated and confirmed by kanamycin-resistance and genomic PCR amplification of SPAE. Protein gel blot also demonstrated sweet potato SPAE expression in these transgenic plants. Phenotypic analysis showed that ...
The C10 family of cysteine proteases includes enzymes that contribute to the virulence of bacterial pathogens, such as SpeB in Streptococcus pyogenes. The presence of homologues of cysteine protease genes in human commensal organisms has not been examined. Bacteroides fragilis is a member of the dominant Bacteroidetes phylum of the human intestinal microbiota, and is a significant opportunistic pathogen. Four homologues of the streptococcal virulence factor SpeB were identified in the B. fragilis genome. These four protease genes, two were directly contiguous to open reading frames predicted to encode staphostatin-like inhibitors, with which the protease genes were co-transcribed. Two of these protease genes are unique to B. fragilis 638R and are associated with two large genomic insertions. Gene annotation indicated that one of these insertions was a conjugative Tn-like element and the other was a prophage-like element, which was shown to be capable of excision. Homologues of the B. fragilis C10
Streptococcal pyrogenic exotoxin B (SPE B), a conserved extracellular cysteine protease expressed by the human pathogenic bacterium Streptococcus pyogenes, was purified and shown to cleave inactive human interleukin 1 beta precursor (pIL-1 beta) to produce biologically active IL-1 beta. SPE B cleaves pIL-1 beta one residue amino-terminal to the site where a recently characterized endogenous human cysteine protease acts. IL-1 beta resulting from cleavage of pIL-1 beta by SPE B induced nitric oxide synthase activity in vascular smooth muscle cells and killed of the human melanoma A375 line. Two additional naturally occurring SPE B variants cleaved pIL-1 beta in a similar fashion. By demonstrating that SPE B catalyzes the formation of biologically active IL-1 beta from inactive pIL-1 beta, our data add a further dimension to an emerging theme in microbial pathogenesis that bacterial and viral virulence factors act directly on host cytokine pathways. The data also contribute to an enlarging ...
The parasitic protozoon Leishmania mexicana possesses an abundance of developmentally regulated cathepsin L-like cysteine proteinases expressed at highest levels in amastigotes. We recently characterised lmcpa, a single-copy gene encoding one such proteinase, LmCPa, which differs from other homologues by possessing a 3-amino-acid insertion at the amino terminal of the predicted mature proteinase. To investigate the role of LmCPa in L. mexicana, we used gene-targeting of promastigotes with hygromycin- and phleomycin-resistance markers to generate null mutants by disrupting sequentially both alleles of lmcpa. The promastigote null mutants did not differ significantly from wild-type L. mexicana in growth rate or morphology and could differentiate to metacyclics and the amastigote-like form, both of which could infect the J774G8 macrophage-like cell line. The null mutant amastigote-like form obtained from the J774G8 cells could also establish rump lesions in CBA mice. By these criteria, therefore, ...
Fingeravtryck Fördjupa i forskningsämnen för Papain-like cysteine proteinase zone (PCP-zone) and PCP structural catalytic core (PCP-SCC) of enzymes with cysteine proteinase fold. Tillsammans bildar de ett unikt fingeravtryck. ...
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six ...
The objective is to determine the presence of cysteine protease gene in the cDNA fragment being synthesized and determining the efficiency of the 3RACE PCR approach for amplification of cDNA end. Morinda citrifolia is from the family Rubiaceae. It is the plant with great medicinal values. The property of this plant has not been characterized thoroughly in previous time. Cysteine protease play important role in plant growth and development in addition to protein degradation process in plant. Better understanding of the biochemical properties will be attained through the study of cysteine protease gene. The amino acids sequences of this enzyme govern the functional characteristic of this enzyme. Therefore, the termini of the cDNA encoding cysteine protease are amplified through Rapid Amplification of cDNA ends (RACE). This experiment was to amplify the 3 terminal of the cDNA nucleotide sequence. The RNA extraction was the preliminary step of the reverse transcription reaction to get the coding ...
Papain-like cysteine proteases are important for the survival of the flagellated protozoa Trypanosoma cruzi, the causative agent of Chagas Disease. the lysosomal cysteine protease designated as cruzipain or cruzain, is the archetype of a multigene family of related isoforms. We investigated the substrate specificity of the cruzipain 2 isoform using internally quenched fluorogenic substrates. We found that cruzipain 2 and cruzain differ substantially regarding the specificity in the S-2, S-1() and S-2() pockets. Our study indicates that cruzipain 2 has a more restricted specificity than cruzain, suggesting that these isoforms might act on distinct natural substrates ...
Proteasome activator complex subunit 3 is a protein that in humans is encoded by the PSME3 gene. The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S ...
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This gene encodes a non-ATPase subunit of the 19S regulator base that functions as a chaperone protein during 26S proteasome assembly. [provided by RefSeq, Jul 2012 ...
Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers. The MEROPS protease classification system counts 14 superfamilies plus several currently unassigned families (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent convergent evolution of the catalytic mechanism. For superfamilies, P = superfamily containing a mixture of nucleophile class families, C = purely cysteine proteases. superfamily. Within each superfamily, ...
Background: The proteasome system has a pivotal role in the control of the immune response, which suggests that it might be involved in the pathogenesis of autoimmune disorders.Objective: To investigate the expression profile of selected proteasomal genes in human peripheral blood mononuclear cells in patients with a variety of autoimmune diseases compared with healthy subjects.Methods: Real time quantitative RT-PCR was used to analyse the mRNA expression pattern of the proteasome activator subunits PA28\textgreeka and PA28\textgreekb and of constitutive proteasome and interferon-\textgreekg-inducible immunoproteasome subunits in peripheral blood mononuclear cells. Simultaneously, protein expression of selected proteasome subunits was quantified by immunoblotting.Results: Under systemic inflammatory conditions the proteasome subunits LMP2 (\textgreekb1i), LMP7 (\textgreekb5i), MECL1 (\textgreekb2i), and PA28\textgreeka were expressed abundantly at the protein level in the vast majority of ...
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). The 3D structure and substrate specificity of the zmCP1 is still unknown. This study is the first one to build the 3D structure of zmCP1 by computer-assisted homology modeling. In order to determine the substrate specificity of zmCP1, docking study is used for rapid and convenient analysis of large populations of ligand-enzyme complexes. Docking results show that zmCP1 has preference for P1 position and P2 position for Arg and a large hydrophobic residue (such as Phe). Gly147, Gly191, Cys189, and Asp190 are predicted to function as active residues at the S1 subsite, and the S2 subsite contains Leu283, Leu193, Ala259, Met194, and Ala286. SIFt results indicate that Gly144, Arg268, Trp308, and Ser311 play important roles in substrate binding. Then Molecular Mechanics-Poisson-Boltzmann Surface Area (MM-PBSA) method was used to
There are no substantial differences between the structures of the enzyme in the free and in the complexed state. The substrate-analog inhibitor binds in the shallow substrate-binding site at the surface of the proteinase, between domains I and II (Fig. 3A). The residues Val-Asn-Ser-Thr-Leu-Gln occupy, and thereby define, the subsites S6 to S1 of the proteinase. Residues P5 to P3 form an antiparallel β sheet with segment 164 to 167 of the long strand eII on one side, and they also interact with segment 189 to 191 of the loop linking domains II and III on the other (Fig. 3A). The functional importance of this latter interaction is supported by the complete loss of proteolytic activity upon deletion of the loop region in TGEV Mpro (8).. In coronavirus Mpro polyprotein cleavage sites, the P1 position is invariably occupied by Gln. At the very bottom of the Mpro S1 subsite, the imidazole of His162 is suitably positioned to interact with the P1 glutamine side chain (Fig. 3, A and B). The required ...
Description: The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been ...
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome. Plays a pivotal role in development of CD8-positive T-cells.
The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. [provided by RefSeq, Jul 2008 ...
2GT8: Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each protomer) in the space group P43212
Caspase 3 (Apopain or Cysteine Protease CPP32 or Protein Yama or SREBP Cleavage Activity 1 or CASP3 or EC 3.4.22.56) - Pipeline Review, H1 2017 Size and Share Published in 2017-05-30 Available for US$ 3500 at Researchmoz.us
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Mediates the association of the SCF(TIR1) E3 ubiquitin ligase complex with the proteasome.
Almost all protease families have been associated with plant development, particularly senescence, which is the final developmental stage of every organ before cell death. Proteolysis remobilizes and recycles nitrogen from senescent organs that is required, for example, seed development. Senescence-associated expression of proteases has recently been characterized using large-scale gene expression analysis seeking to identify and characterize senescence-related genes. Increasing activities of proteolytic enzymes, particularly cysteine proteases, are observed during the senescence of legume nodules, in which a symbiotic relationship between the host plant and bacteria (Rhizobia) facilitate the fixation of atmospheric nitrogen. It is generally considered that cysteine proteases are compartmentalized to prevent uncontrolled proteolysis in nitrogen-fixing nodules. In addition, the activities of cysteine proteases are regulated by endogenous cysteine protease inhibitors called cystatins. These small proteins
The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the peptidase T1A family, that is a 20S core alpha subunit. Two alternative transcripts encoding different isoforms have been identified. [provided by RefSeq, Jul 2008] ...
Proteasomes can exist in several different molecular forms in mammalian cells. The core 20S proteasome, containing the proteolytic sites, binds regulatory complexes at the ends of its cylindrical structure. Together with two 19S ATPase regulatory complexes it forms the 26S proteasome, which is involved in ubiquitin-dependent proteolysis. The 20S proteasome can also bind 11S regulatory complexes (REG, PA28) which play a role in antigen processing, as do the three variable γ-interferon-inducible catalytic β-subunits (e.g. LMP7). In the present study, we have investigated the subcellular distribution of the different forms of proteasomes using subunit specific antibodies. Both 20S proteasomes and their 19S regulatory complexes are found in nuclear, cytosolic and microsomal preparations isolated from rat liver. LMP7 was enriched approximately two-fold compared with core α-type proteasome subunits in the microsomal preparations. 20S proteasomes were more abundant than 26S proteasomes, both in ...
Proteasome subunit beta type ; The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (245 aa ...
PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in complex with Z4444621910 (Mpro-x2569 ...
Destruction of cancer cells by cytotoxic T lymphocytes depends on immunogenic tumor peptides generated by proteasomes and presented by human leukocyte antigen (HLA) molecules. Functional differences arising from alleles of immunoproteasome subunits have not been recognized so far. We analyzed the genetic polymorphism of the immunoproteasome subunits LMP2 and LMP7 and of the transporters associated with antigen processing (TAP1 and TAP2) in two independently collected panels of colorectal carcinoma patients (N1 = 112, N2 = 62; controls, N = 165). High risk of colon cancer was associated with the LMP7-K/Q genotype (OR = 8.10, P = 1.10 × 10−11) and low risk with the LMP7-Q/Q genotype (OR = 0.10, P = 5.97 × 10−13). The basis for these distinct associations of LMP7 genotypes was functionally assessed by IFN-γ stimulation of colon carcinoma cell lines (N = 10), followed by analyses of mRNA expression of HLA class I, TAP1, TAP2, and LMP7, with real-time PCR. Whereas induction of HLA-B, TAP1, and ...
The Ubiquitin-proteasome system is responsible for the regulated protein degradation in eucaryotic cells. The 20S proteasome is as a multicatalytic protease the central complex of these system. This study has shown that it is possible to separate 20S proteasome subtypes from HeLa cells by chromatography. 20s proteasome subtypes differ in structure and proteolytic activity. The subtype-pattern and the activity are significantly changed after an induction of the cells with gamma-Interferon (gamma-IFN) under formation of immuno proteasomes. After gamma-IFN induction mainly mixed complexes have been formed with both constitutive and immuno subunits. Further it has been shown that in cell compartements cytoplasm, microsomes and nucleus of HeLaS3 cells different 20S proteasome subtypes are located. Among other things glycosylation of some subunits is responsible for that phenomenon. With regard to new strategies in diagnostic and therapy of human diseases the exactly knowledge of structure and ...
TY - JOUR. T1 - Base-CP proteasome can serve as a platform for stepwise lid formation. AU - Yu,Zanlin. AU - Livnat-Levanon,Nurit. AU - Kleifeld,Oded. AU - Mansour,Wissam. AU - Nakasone,Mark A.. AU - Castaneda,Carlos A.. AU - Dixon,Emma K.. AU - Fushman,David. AU - Reis,Noa. AU - Pick,Elah. AU - Glickman,Michael H.. PY - 2015. Y1 - 2015. N2 - 26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid sub-complexes. Even within the lid, subunits have been demarcated into two modules: module 1 (Rpn5, Rpn6, Rpn8, Rpn9 and Rpn11), which interacts with both CP and base sub-complexes and module 2 (Rpn3, Rpn7, Rpn12 and Rpn15) that is attached mainly to module 1. We now show that suppression of RPN11 expression halted lid assembly yet enabled the base and 20S CP to pre-assemble and form a base-CP. A key role for Regulatory particle non-ATPase 11 (Rpn11) in bridging lid ...
In-Silico Identification of Potent Inhibitors of COVID-19 Main Protease (Mpro) and Angiotensin Converting Enzyme 2 (ACE2) from Natural Products: Quercetin, Hispidulin, and Cirsimaritin Exhibited Better Potential Inhibition than Hydroxy-Chloroquine Against COVID-19 Main Protease Active Site and ACE2
Articles Thomas, S. R.et al. 2020. Exploring the chemoselectivity towards cysteine arylation by cyclometalated Au(III) compounds: new mechanistic insights. ChemBioChem (10.1002/cbic.202000262) Santi et al. 2020. Streptavidin-hosted Organocatalytic Aldol Addition. Molecules, just accepted. Tang et al. 2020. Use of an Asparaginyl Endopeptidase for Chemo-enzymatic Peptide and Protein labeling. Chem Science, just accepted. Nödling, A. R.et al. 2020. Enabling protein-hosted organocatalytic transformations. RSC…
PA700 proteasome activator: high MW, ATP-dependent activator of 20 S proteasome; MW 700 kDa; composed of 16 peptides ranging in MW from 20-100 kDa
Dynamical properties of enzyme-substrate complexes disclose substrate specificity of the SARS-CoV-2 main protease as characterized by the electron density ...
Relationship of the surface export of SDH and SpeB secretion. (A) Determination of the relative cysteine protease activities of SpeB present in the culture supe
4EKF: Regulation of a Viral Proteinase by a Peptide and DNA in One-dimensional Space: III. ATOMIC RESOLUTION STRUCTURE OF THE NASCENT FORM OF THE ADENOVIRUS PROTEINASE.
Fingerprint Dive into the research topics of Evidence for a role of immunoproteasomes in regulating cardiac muscle mass in diabetic mice. Together they form a unique fingerprint. ...
Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12 ...
Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases. ...
The 26S proteasome is a multicatalytic proteise complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator.The…
SWISS-MODEL Template Library (SMTL) entry for 1pau.1. Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO
the constitute families differ by insertion into and circular permutation of the common catalytic core made of one alpha-helix and 3-strands of beta- ...
SiliaBond® Cysteine (Si-Cys) is the silica bound equivalent of the amino acid Cysteine. By attaching the molecule to the backbone via the amino group, the thiol group remains free and accessible for higher metal scavenging efficiency.
This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... 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 ...
... is a human lysosomal cysteine endopeptidase. Cathepsin L2 Brömme D, Li Z, Barnes M, Mehler E (February 1999). " ... Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C (April 1998). "Cathepsin L2, a novel human cysteine ...
Shows weak endopeptidase activity Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). Nägler DK, Zhang ... Santamaría I, Velasco G, Pendás AM, Fueyo A, López-Otín C (July 1998). "Cathepsin Z, a novel human cysteine proteinase with a ... Nägler DK, Ménard R (August 1998). "Human cathepsin X: a novel cysteine protease of the papain family with a very short ... Cathepsin X (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, ...
Takahashi K, Nishii W, Shibata C (2012). "The digestive fluid of Drosera indica contains a cysteine endopeptidase ("droserain ... The names cephalotusin, dionaeasin and droserasin have been proposed for similar aspartic endopeptidases originating from the ...
... clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Lett. 441 (3): 361-5. doi:10.1016/S0014-5793(98) ... 1999). "An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation". Nature. 396 (6712): 695-9. ... Tanaka T, Inazawa J, Nakamura Y (Dec 1996). "Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and ... This gene encodes a cysteine protease, legumain, that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme ...
... is cleaved by several proteases including Separase and Calcium-dependent cysteine endopeptidase Calpain-1 during mitosis ... and its dissolution by the cysteine protease Separase at the metaphase to anaphase transition results in the separation of ...
... is also known to play a role in axon regeneration and has an additional DISC1-modulated function as a cysteine endopeptidase. ...
... (EC 3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is ... Cysteine Peptidases of Mammals: Their Biological Roles and Potential Effects in the Oral Cavity and Other Tissues in Health and ... Venkatesh K, Prasanth B, Rajesh P, Annie JG, Mukesh P, Jesu A (2014). "A murrel cysteine protease, cathepsin L: bioinformatics ... Barrett, A.J.; Buttle, D.J.; Mason, R.W. (1988). "Lysosomal cysteine proteinases". ISI Atlas of Science. Biochemistry. 1: 256- ...
It is of a family of proteases known as the cysteine endopeptidases, a group that also includes papain derived from papaya ... doi:10.1016/0076-6879(70)19020-3. Brocklehurst K, Willenbrock F, Salih E (1987). "Cysteine proteinases". In Neuberger A, ...
... cysteine endopeptidases MeSH D08.811.277.656.300.215.096 - bromelains MeSH D08.811.277.656.300.215.120 - calpain MeSH D08.811. ... endopeptidase clp MeSH D08.811.277.656.149.500 - protease la MeSH D08.811.277.656.300 - endopeptidases MeSH D08.811.277.656. ... endopeptidase clp MeSH D08.811.277.656.300.760.247 - endopeptidase k MeSH D08.811.277.656.300.760.284 - enteropeptidase MeSH ... 300.066 - aspartic endopeptidases MeSH D08.811.277.656.300.066.180 - cathepsin d MeSH D08.811.277.656.300.066.185 - cathepsin e ...
This cysteine endopeptidase is coded by adenoviruses. Webster A, Hay RT, Kemp G (January 1993). "The adenovirus protease is ...
... (EC 3.4.22.44, Tobacco Etch Virus nuclear-inclusion-a endopeptidase) is a highly sequence-specific cysteine ... Bazan JF, Fletterick RJ (November 1988). "Viral cysteine proteases are homologous to the trypsin-like family of serine ... TEV protease uses a cysteine as its catalytic nucleophile (as do many other viral proteases). Covalent catalysis is performed ...
... prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer peptide ...
... paired-basic endopeptidase, yeast cysteine proteinase F, paired-basic endopeptidase, andrenorphin-Gly-generating enzyme, ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (October 1988). "Yeast KEX2 genes encodes an endopeptidase homologous to ... Mizuno K, Nakamura T, Ohshima T, Tanaka S, Matsuo H (February 1989). "Characterization of KEX2-encoded endopeptidase from yeast ... "Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast ...
The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine+endopeptidases at the US National ... In fact, dozens of latices of different plant families are known to contain cysteine proteases. Cysteine proteases are used as ... Plant cysteine proteases isolated from these plants have been found to have high proteolytic activities that are known to ... Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. These proteases share a common catalytic ...
... is synthesized as an inactive zymogen. AEP and other cysteine peptidase are activated when pH changes ... Legumain is a cysteine protease from the C13 family of the CD clan of proteases (MEROPS). It uses a catalytic triad of Cysteine ... 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) ...
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 ... Glutamyl endopeptidase can inhibit the activation of targets within the complement system. It is indicated to cause inhibition ...
Birktoft, Jens J.; Breddam, Klaus (1994). "[8] Glutamyl endopeptidases". Proteolytic Enzymes: Serine and Cysteine Peptidases. ... subtilis glutamyl endopeptidase GluBS Enterococcus E. faecalis glutamyl endopeptidase SprE Glutamyl endopeptidase is in at ... S. epidermidis glutamyl endopeptidase GluSE Also called S. epidermidis serine protease (Esp). S. warneri glutamyl endopeptidase ... Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been ...
Buttle DJ, Kembhavi AA, Sharp SL, Shute RE, Rich DH, Barrett AJ (July 1989). "Affinity purification of the novel cysteine ... Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, chymopapain, Papaya ... Glycyl+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Biology portal. ...
Cysteine peptidases belonging to MEROPS peptidase family C51 (D-alanyl-glycyl endopeptidase, clan CA). Rigden DJ, Jedrzejas MJ ... The CHAP domain contains two invariant residues, a cysteine and a histidine. These residues form part of the putative active ... It has been suggested that CHAP domain containing proteins utilise a catalytic cysteine residue in a nucleophilic-attack ... The domain is named after the acronym cysteine, histidine-dependent amidohydrolases/peptidases. Many of these proteins are ...
... 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 ... Santamaría I, Velasco G, Pendás AM, Fueyo A, López-Otín C (July 1998). "Cathepsin Z, a novel human cysteine proteinase with a ... "Entrez Gene: CTSZ cathepsin Z". Turk V, Stoka V, Vasiljeva O, Renko M, Sun T, Turk B, Turk D (January 2012). "Cysteine ...
Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... 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 ... In fact, dozens of latices of different plant families are known to contain cysteine proteases.[1] Cysteine proteases are used ...
C-aaX in which C is an S-isoprenylated cysteine residue, a is usually aliphatic and X is the C-terminal residue of the ... 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) Biology portal. ...
cysteine-type endopeptidase activity. • cysteine-type peptidase activity. • hydrolase activity. Cellular component. • lysosome ... 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: ... Linnevers C, Smeekens SP, Bromme D (May 1997). "Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ ...
serine-type endopeptidase activity. • cysteine-type endopeptidase activity. • aspartic-type endopeptidase activity. ... Lenarcic B, Kos J, Dolenc I, Lucovnik P, Krizaj I, Turk V (July 1988). "Cathepsin D inactivates cysteine proteinase inhibitors ...
cysteine-type endopeptidase activity involved in apoptotic process. • tumor necrosis factor receptor binding. • cysteine-type ... 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 signaling pathway. • response to antibiotic. • ...
cysteine-type endopeptidase activity. • hydrolase activity. • identical protein binding. Cellular component. • cytoplasm. • ... Cysteine 464 and histidine 414 are crucial for this activity. Like metacaspases, the paracaspase cleaves substrates after an ...
... inhibitor of cysteine proteases Camostat - inhibitor of trypsin and various other proteases Ecallantide - kallikrein inhibitor ... An endopeptidase inhibitor is a drug that inhibits one or more endopeptidase enzymes. Endopeptidases are one of two types of ... Endopeptidases cleave peptide bonds of non-terminal amino acids (that is, they cut proteins/peptides into two chains), whereas ... Some examples of endopeptidase inhibitors include the following: Neprilysin inhibitors Selective neprilysin inhibitors ...
... calicivirus trypsin-like cysteine protease, calicivirus TCP, calicivirus 3C-like protease, calicivirus endopeptidase, rabbit ... Meyers G, Rossi C, Thiel HJ (2004). "Calicivirus endopeptidases". In Barrett AJ, Rawlings ND, Woessner JF (eds.). Handbook of ... This enzyme catalyses the following chemical reaction Endopeptidase with a preference for cleavage when the P1 position is ... hemorrhagic disease virus 3C endopeptidase) is an enzyme. ...
cysteine-type endopeptidase inhibitor activity. • связывание с ионом металла. • ubiquitin-protein transferase activity. • ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • response to amino acid. • negative ... inhibition of cysteine-type endopeptidase activity involved in apoptotic process. • негативная регуляция апоптоза. ...
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 ... Wilk S, Orlowski M (March 1983). "Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease ... adenylylated ubiquitin is then transferred to a cysteine of a second enzyme, ubiquitin-conjugating enzyme (E2). In the last ...
positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • negative regulation of viral ... activation of cysteine-type endopeptidase activity involved in apoptotic process. • tumor necrosis factor-mediated signaling ... Nevertheless, TRADD binds FADD, which then recruits the cysteine protease caspase-8. A high concentration of caspase-8 induces ...
activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c. • cellular respiration. • ... All cytochrome c proteins contain a characteristic CXXCH (cysteine-any-any-cysteine-histidine) amino acid motif that binds heme ... This release of cytochrome c in turn activates caspase 9, a cysteine protease. Caspase 9 can then go on to activate caspase 3 ... the heme group of cytochrome c makes thioether bonds with two cysteine side chains of the protein.[15] One of the main ...
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • negative regulation of hydrogen ... serine-type endopeptidase activity. • protein tyrosine kinase activity. • Ras guanyl-nucleotide exchange factor activity. • ...
... prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer peptide ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... 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 ... Aspartic+Endopeptidases at the US National Library of Medicine Medical Subject Headings (MeSH) ...
... in the sequence cysteine-tyrosine-isoleucine-glutamine-asparagine-cysteine-proline-leucine-glycine-amide (Cys - Tyr - Ile - Gln ... role of aminopeptidases and endopeptidases". Peptides. 12 (5): 1119-25. doi:10.1016/0196-9781(91)90068-z. PMID 1800950.. ... its C-terminus has been converted to a primary amide and a disulfide bridge joins the cysteine moieties.[116] Oxytocin has a ...
positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • positive regulation of G-protein ...
activation of cysteine-type endopeptidase activity involved in apoptotic process. • signal transduction. • apoptotic process. • ... activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • cell-cell signaling. • cell ... positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • immune response. • positive ...
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) ... Retrieved from "https://en.wikipedia.org/w/index.php?title=Proteasome_endopeptidase_complex&oldid=826116286" ...
activation of cysteine-type endopeptidase activity involved in apoptotic process. • response to drug. • signal transduction. • ... Each protein is divided into three domains: an N-terminal extracellular domain with four cadherin-like repeats and a cysteine- ...
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • negative regulation of hydrogen ... serine-type endopeptidase activity. • protein tyrosine kinase activity. • Ras guanyl-nucleotide exchange factor activity. • ...
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • cellular response to mercury ion. ...
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 ... Disulfide bond formation is the creation of disulfide bridges (covalent bonds) between two cysteine amino acids in a chain ... bond.[3] Three common endopeptidases are pepsin, trypsin, and chymotrypsin. Chymotrypsin performs a hydrolysis reaction that ...
cysteine-type endopeptidase inhibitor activity involved in apoptotic process. Component cel·lular. • extracellular region. • ... negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • sodium-independent organic anion ...
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • cellular response to mercury ion. ...
Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and peptide.[1] ... It then attacks the disulphide bond formed between 2 cysteine residues, forming one SH bond and a single S− group. This S− ... Next the adjacent S− group attack disulphide bond in cysteine-SG complex and release the second SG− anion. It receives one ... The NADPH is involved in the generation of FADH-. In the active site, there are two cysteine residues besides the FAD cofactor ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... serine-type endopeptidase activity. Cellular component. • lamellipodium membrane. • extracellular exosome. • lysosomal membrane ...
Cysteine protease. *Aspartic acid protease. *Metalloendopeptidase. *Threonine endopeptidase *Proteasome endopeptidase complex. ... One way to make a nucleophile is by a catalytic triad, where a histidine residue is used to activate serine, cysteine, or ... Serine, threonine and cysteine proteases use a nucleophilic residue (usually in a catalytic triad). That residue performs a ... The mechanism used to cleave a peptide bond involves making an amino acid residue that has the cysteine and threonine ( ...
RI has a surprisingly high cysteine content (~6.5%, cf. 1.7% in typical proteins) and is sensitive to oxidation. RI is also ...
activation of cysteine-type endopeptidase activity involved in apoptotic process. • cell cycle arrest. • Ras protein signal ...
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process. • positive regulation of proteasomal ...
positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • positive regulation of interleukin ... activation of cysteine-type endopeptidase activity involved in apoptotic process. • negative regulation of inflammatory ...
positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway. • negative regulation of ... positive regulation of cysteine-type endopeptidase activity involved in apoptotic process. • protein homotrimerization. ... serine-type endopeptidase complex. Biological process. • cellular response to retinoic acid. • cellular response to heat. • ... serine-type endopeptidase activity. • hydrolase activity. • peptidase activity. • identical protein binding. Cellular component ...
activation of cysteine-type endopeptidase activity involved in apoptotic process. • positive regulation of positive chemotaxis ... serine-type endopeptidase activity. • protease binding. Cellular component. • membrane. • extracellular matrix. • intrinsic ...
Cysteine Proteases and Cell Differentiation: Excystment of the Ciliated Protist Sterkiella histriomuscorum Eduardo Villalobo, ... Use of Recombinant Entamoeba histolytica Cysteine Proteinase 1 To Identify a Potent Inhibitor of Amebic Invasion in a Human ... The Intestinal Protozoan Parasite Entamoeba histolytica Contains 20 Cysteine Protease Genes, of Which Only a Small Subset Is ... Blastocystis ratti Contains Cysteine Proteases That Mediate Interleukin-8 Response from Human Intestinal Epithelial Cells in an ...
Overexpression of the Natural Inhibitor of Cysteine Peptidases in Leishmania mexicana Leads to Reduced Virulence and a Th1 ...
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
... 0-9. A. B. C. D. E. F. G. H. I. J. K. L. M. N. O. P. Q. R. S. T. U ...
Amura Therapeutics is developing small molecule CAC1 cysteine endopeptidase inhibitors its AMcore™ technology platform for the ... Research programme: cysteine endopeptidase inhibitors - Amura Alternative Names: AM-3701; AM-3840; AM-3876 Latest Information ... Mechanism of Action Cathepsin K inhibitors; Cathepsin S inhibitors; Cysteine endopeptidase inhibitors ...
... are a recently identified family of cysteine-class endopeptidases. A single gene encoding a Schistosoma mansoni asparaginyl ... endopeptidase (a.k.a. Sm32 or schistosome legumain) has been reported, but by sequence homology it would be expected to yield ... Asparaginyl endopeptidases, or legumains, are a recently identified family of cysteine-class endopeptidases. A single gene ... Identification of a cDNA encoding an active asparaginyl endopeptidase of Schistosoma mansoni and its expression in Pichia ...
Cysteine Endopeptidases * asparaginylendopeptidase Grant support * R01 AI072429/AI/NIAID NIH HHS/United States ... Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase J ... The first step removes the majority of the ectodomain and can be performed by asparagine endopeptidase (AEP) or cathepsin ...
Plants encode a unique group of papain-type cysteine endopeptidases (CysEP) characterized by a C-terminal KDEL endoplasmic ... 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 ...
Legumains are a recently discovered family of plant and animal cysteine endopeptidases with a cleavage specificity for Asn in ... Legumains are a recently discovered family of plant and animal cysteine endopeptidases with a cleavage specificity for Asn in ... asparagine-specific cysteine endopeptidases, biosynthesis, evolution, legumain, propolypeptide processing, protein degradation ... Legumains - a family of asparagine-specific cysteine endopeptidases involved in propolypeptide processing and protein breakdown ...
Subclass 3.4 (Peptidases) ,, Sub-subclass 3.4.22 (Cysteine endopeptidases) ,, Peptidase 3.4.22.27. ...
cysteine-type endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ...
cysteine-type endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ... Title: Cysteine cathepsins B, X and K expression in peri-arteriolar glioblastoma stem cell niches. ... The protein encoded by this gene is a lysosomal cysteine proteinase involved in bone remodeling and resorption. This protein, ...
This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. The various forms of peptidase 1 ... which bind to the cysteine active site and block substrate access. The major kiwifruit cysteine proteinase inhibitor KCPI1 has ... 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 ...
Cysteine Endopeptidases / physiology*. DNA / biosynthesis, isolation & purification. DNA Fragmentation. Electrophoresis, ... 0/Hallucinogens; 0/Proto-Oncogene Proteins c-bcl-2; 1972-08-3/Tetrahydrocannabinol; 9007-49-2/DNA; EC 3.4.22.-/Cysteine ...
Two events, high metacestode viability (100%) and high cysteine protease activity were found to be ... Cysteine Endopeptidases / metabolism. Cysticercosis / immunology, parasitology, veterinary*. DNA Fragmentation. Flow Cytometry ... 0/Annexin A5; 0/Culture Media; 0/Fluorescent Dyes; EC 3.4.22.-/Cysteine Endopeptidases ... Two events, high metacestode viability (100%) and high cysteine protease activity were found to be closely related to a high ...
Cysteine Endopeptidases); EC 3.4.22.37 (argingipain, Porphyromonas gingivalis). ... Ciste na Endopeptidases/qu mica. C lulas Epiteliais/microbiologia. Flavonoides/isolamento & purifica o. cido G lico/qu mica. ...
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. ...
Cysteine endopeptidases. BRITE hierarchy. Reaction(IUBMB). Broad endopeptidase specificity. Comment. In peptidase family C2. ...
Cysteine Endopeptidases); EC 3.4.22.28 (3C proteases); EC 3.5.4.1 (Cytosine Deaminase). ... Ciste na Endopeptidases/gen tica. Ciste na Endopeptidases/metabolismo. Citosina Desaminase/gen tica. Citosina Desaminase/ ... Ciste na Endopeptidases/bioss ntese. Citosina Desaminase/bioss ntese. Flucitosina/farmacologia. Terapia Gen tica/m todos. V rus ...
A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine ... clostripain and gingipains in a new clan of cysteine endopeptidases.. FEBS Lett. 441 361-5 1998 ...
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 ... T1 - Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. latex displaying ...
Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in ... Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in ... Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in ... Ricinosomes are specialized ER-derived organelles that store the inactive pro-forms of KDEL-tailed cysteine endopeptidases ( ...
Cysteine endopeptidase assay.Cysteine protease activity present in ammonium sulfate-precipitated culture supernatants was ... The cysteine protease-specific inhibitor, E64 (Sigma), was included in parallel assays at a concentration of 1 μM to determine ... A role for trigger factor and an Rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase ... In addition, analysis of β-hemolysis, streptokinase production, and secretion of a cysteine protease were included in the ...
Cathepsin V is a human lysosomal cysteine endopeptidase. Cathepsin L2 Brömme D, Li Z, Barnes M, Mehler E (February 1999). " ... Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C (April 1998). "Cathepsin L2, a novel human cysteine ...
negative regulation of cysteine-type endopeptidase activity. down. 2.80E-06. Enrichment of Gene Ontology (GO) in DEGs was ...
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR ...
Redirected from Cysteine endopeptidase) Cysteine proteases, also known as thiol proteases, are enzymes that degrade proteins. ... 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 ... In fact, dozens of latices of different plant families are known to contain cysteine proteases.[1] Cysteine proteases are used ...
cysteine-type endopeptidase activity Source: InterPro. *serine-type peptidase activity Source: UniProtKB-KW ...
cysteine-type endopeptidase activity Source: MGI. *cysteine-type peptidase activity Source: MGIInferred from sequence orthology ... p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues ...
cysteine-type endopeptidase activity Source: InterPro. Complete GO annotation on QuickGO .... ,p>This section provides ...
  • The tryptic peptide mass fingerprint of quercifoliain I analyzed with the MASCOT search tool did not find a match with papain or any other plant cysteine proteases. (uab.cat)
  • 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)
  • Recently, analysis of the crystal structure of the zymogen showed that the catalytic domain of SpeB is structurally similar to the papain superfamily of cysteine proteases but differs in the propeptide region ( 30 ). (asm.org)
  • As a cysteine protease, peptidase 1 functions by cleaving other mite proteases in a biochemical cascade that results in the activation of other allergens. (wikipedia.org)
  • After evaluating many fluorescent substrates, we chose assay substrates for cysteine proteases (papain) and serine proteases (trypsin) and used mouse pancreatic extract (1mg/mL) as the positive control. (thermofisher.com)
  • They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. (creativebiomart.net)
  • Stathopoulos C (1998) Structural features, physiological roles, and biotechnological applications of the membrane proteases of the OmpT bacterial endopeptidase family: a micro-review. (wordnik.com)
  • Metalloproteinases, serine proteases, and cysteine proteases were blocked to measure their relative implication in elastin degradation. (ahajournals.org)
  • 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)
  • 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)
  • 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 that are N-terminal nucleophile hydrolases are included in clan PB. (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)
  • Previous studies have focused on individual enzymes in particular species and identified mainly cysteine peptidases (e.g. (pubmedcentralcanada.ca)
  • Peptidases of other classes are also expressed in the tick gut, e.g. a leucine metallo-aminopeptidase and a hemolytic serine endopeptidase found in cytoplasm and lumen, respectively (e.g. (pubmedcentralcanada.ca)
  • The protein encoded by this gene is a lysosomal cysteine proteinase involved in bone remodeling and resorption. (nih.gov)
  • The protein encoded by this gene, a member of the peptidase C1 family, is a lysosomal cysteine proteinase that may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. (genecards.org)
  • Alternatively, we hypothesized that a truncated M protein may interfere with processing of this secreted protease, and therefore we tested cysteine protease activity in genetically defined mutant strains that express either no M protein or membrane-anchored M protein with an in-frame deletion of the AB repeat region. (asm.org)
  • Therefore, we conclude that M protein is not required for maturation of the streptococcal cysteine protease SpeB. (asm.org)
  • Peptidase 1 is a cysteine protease belonging to the C1 protein family, with a structure similar to that of papain. (wikipedia.org)
  • Asparaginyl endopeptidase (AEP or legumain) is a lysosomal cysteine protease that cleaves protein substrates on the C-terminal side of asparagine. (pnas.org)
  • The cystatins: protein inhibitors of cysteine proteinases. (embl-heidelberg.de)
  • The last decade has witnessed enormous progress of protein inhibitors of cysteine proteinases concerning their structures, functions and evolutionary relationships. (embl-heidelberg.de)
  • Several hormone-related proteins were prominently featured in differentiated calli as compared with the initiated calli, such as alpha-amylase isoforms, mannose-binding rice lectin, putative dehydration stress-induced protein, cysteine endopeptidase and cystatin. (deepdyve.com)
  • This is also supported by an enrichment of protein functions such as cysteine-type endopeptidase activity, lysozyme activity, or lipase activity. (wordnik.com)
  • This enzyme is a lysosomal cysteine protease with both endopeptidase and exopeptidase activity that may play a role in protein turnover. (cancerindex.org)
  • Legumains are a recently discovered family of plant and animal cysteine endopeptidases with a cleavage specificity for Asn in the P1 position of peptide bonds. (naver.com)
  • Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L. (genome.jp)
  • Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. (proteopedia.org)
  • The constriction of this subsite in glycyl endopeptidase explains the unique specificity of this enzyme for cleavage after glycyl residues and is a major component of its resistance to inhibition by cystatins. (proteopedia.org)
  • Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity. (proteopedia.org)
  • This enzyme exhibits cysteine protease activity with broad endopeptidase specificity. (wikipedia.org)
  • Cysteine protease inhibitors block schistosome hemoglobin degradation in vitro and decrease worm burden and egg production in vivo (1996) Wasilewski Margaret M et al. (naver.com)
  • Cystatins are a family of cysteine protease inhibitors that occur mainly as single domain proteins. (embl-heidelberg.de)
  • Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. (embl-heidelberg.de)
  • Recently determined crystal structures of chicken cystatin and human stefin B established a new mechanism of interaction between cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinases and their inhibitors. (embl-heidelberg.de)
  • Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. (creativebiomart.net)
  • The first step removes the majority of the ectodomain and can be performed by asparagine endopeptidase (AEP) or cathepsin family members. (nih.gov)
  • Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. (genome.jp)
  • Z-Val-Arg-NHMec) Cathepsin V is a human lysosomal cysteine endopeptidase. (wikipedia.org)
  • Heparin modulates the endopeptidase activity of leishmania mexicana cysteine protease cathepsin L-Like rCPB2. (google.es)
  • The degradation pathway is initiated by endopeptidases of aspartic and cysteine class (cathepsin D supported by cathepsin L and legumain) and continued by cysteine amino- and carboxy-dipeptidases (cathepsins C and B). The identified enzymes are potential targets to developing novel anti-tick vaccines. (pubmedcentralcanada.ca)
  • Testing the RPMI medium used for washing away inflammatory cells from metacestodes with 100% viability, with the fluorescent substrate Z-Phe-Ala-AFC for measuring cysteine protease activity, significant fluorescent values were found. (biomedsearch.com)
  • 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)
  • It had the following phenotypes: decreased β-hemolysis mediated by streptolysin S, reduction in the activity of a secreted cysteine protease and streptokinase, and an altered immunoglobulin and fibrinogen-binding phenotype. (asm.org)
  • GO annotations related to this gene include peptidase activity and cysteine-type peptidase activity . (genecards.org)
  • Predicted to have cysteine-type endopeptidase inhibitor activity. (jax.org)
  • Predicted to have cysteine-type endopeptidase activity and thiol-dependent ubiquitin-specific protease activity. (mcw.edu)
  • The streptococcal pyrogenic exotoxin B (SpeB) is an important virulence factor of group A streptococci (GAS) with cysteine protease activity. (asm.org)
  • Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. (naver.com)
  • 2007) IrAE: an asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus. (wordnik.com)
  • Crystal structure of the cysteine peptidase papain in complex with its covalent inhibitor E-64. (wikipedia.org)
  • The structure of the S1 substrate binding site of glycyl endopeptidase differs from that of papain by the substitution of glycines at residues 23 and 65 in papain, with glutamic acid and arginine, respectively, in glycyl endopeptidase. (proteopedia.org)
  • By the end of the decade, it was suspected that Der p 1 was a cysteine protease when its structure showed similarities to that of actinidin and papain. (wikipedia.org)
  • Plant-specific papain-type KDEL-tailed cysteine endopeptidases (KDEL-CysEPs or CEPs) have been shown to be involved in PCD during vegetative development as executors for the last step in the process. (uni-regensburg.de)
  • Porphyromonas gingivalis , the major etiologic agent of chronic periodontitis, produces a broad spectrum of virulence factors, including Arg- and Lys-gingipain cysteine proteinases. (mdpi.com)
  • Arg- and Lys-gingipain cysteine proteinases are the main endopeptidases produced by P. gingivalis and are both extracellular and cell-bound [ 5 ]. (mdpi.com)
  • Calpains are a family of cytosolic cysteine proteinases. (embl.de)
  • Cysteine protease required for autophagy, which cleaves the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP, allowing the liberation of form I. A subpopulation of form I is subsequently converted to a smaller form (form II). (abcam.com)
  • 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)
  • Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently bound to the catalytic Cys 25. (proteopedia.org)
  • Due to its cysteine protease structure, Der p 1 may be irreversibly inhibited by E-64 or iodoacetamide, which bind to the cysteine active site and block substrate access. (wikipedia.org)
  • Cleavage of the cysteine protease substrate results in fluorescence at 460nm, and cleavage of the serine protease results in fluorescence at 520nm. (thermofisher.com)
  • These homologous endopeptidases belong to the large family of proteins called caspases (cysteine-dependent aspartate-specific protease). (hindawi.com)
  • 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)
  • Amphiphysin I is cleaved by a cysteine proteinase asparagine endopeptidase (AEP) at N278 in the brains of AD patients. (elifesciences.org)
  • A single gene encoding a Schistosoma mansoni asparaginyl endopeptidase (a.k.a. (nih.gov)
  • Asparaginyl endopeptidase of jack bean seeds. (naver.com)
  • The team's previous work had led them to suggest that an enzyme called 'asparaginyl endopeptidase ' (AEP) could potentially be responsible for breaking down L-asparaginase and triggering allergic reactions in some children treated with the drug. (wordnik.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)
  • Peptidase 1 (mite) (EC 3.4.22.65), also known as endopeptidase 1 (mite), is an enzyme found in various species of mites. (wikipedia.org)
  • PL-3994 has an extended half-life, with reduced affinity for natriuretic peptide clearance receptors and increased resistance to neutral endopeptidase , an endogenous enzyme that degrades natriuretic peptides. (wordnik.com)
  • Further expression analysis revealed that the induction of genes encoding alcohol dehydrogenase 3, metalloprotease FtsH, cysteine protease 1 precursor, phytepsin precursor (aspartic protease), and a 26S proteasome regulatory subunit was associated with the androgenic potential of microspores, whereas the induction of transcripts involved in signaling and cytoprotection was associated with stress responses. (tudelft.nl)
  • endopeptidases (serine, aspartic, cysteine and metalloproteinases) cleave the peptide distal to the terminus. (thermofisher.com)
  • Apoptosis of lymphocytes in the inflammatory reaction around Taenia solium metacestodes, might have been induced by the parasite cysteine protease, and may be involved in impairing cell-mediated immune responses in human and porcine cysticercosis. (biomedsearch.com)
  • 2003) The cytosolic endopeptidase , thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation. (wordnik.com)
  • The gene encoding the streptococcal cysteine protease (streptococcal pyrogenic exotoxin B), speB , is present in most isolates of GAS and is highly conserved among them ( 52 ). (asm.org)
  • Asparaginyl endopeptidases, or legumains, are a recently identified family of cysteine-class endopeptidases. (nih.gov)
  • Reaction mechanism of the cysteine protease mediated cleavage of a peptide bond. (wikipedia.org)
  • Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. (uab.cat)
  • Fingerprint Dive into the research topics of 'Purification and characterization of a cysteine endopeptidase from vasconcellea quercifolia A. St.-Hil. (uab.cat)
  • Quantification of a dual angiotensin I-converting enzyme-neutral endopeptidase inhibitor and the active thiol metabolite in dog plasma by high-performance liquid chromatography with ultraviolet absorbance detection. (childrensmercy.org)