Chemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
Cysteine EndopeptidasesCathepsin BCysteineAmino Acid SequenceMolecular Sequence DataEndopeptidasesNeprilysinSerine EndopeptidasesThiorphanPHEX Phosphate Regulating Neutral EndopeptidaseProtease InhibitorsCysteine ProteasesMetalloendopeptidasesCysteine Proteinase InhibitorsCysteine DioxygenaseSubstrate SpecificityCysteine SynthaseGlycopeptidesDisulfidesNeurotensinSerine Proteinase InhibitorsHydrolysisKineticsDipeptidesLysostaphinAspartic Acid EndopeptidasesCathepsinsSulfhydryl CompoundsBase SequenceChromatography, High Pressure Liquid
Cysteine Endopeptidases
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
Cathepsin B
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
Cysteine
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Amino Acid Sequence
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Endopeptidases
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
Neprilysin
Enzyme that is a major constituent of kidney brush-border membranes and is also present to a lesser degree in the brain and other tissues. It preferentially catalyzes cleavage at the amino group of hydrophobic residues of the B-chain of insulin as well as opioid peptides and other biologically active peptides. The enzyme is inhibited primarily by EDTA, phosphoramidon, and thiorphan and is reactivated by zinc. Neprilysin is identical to common acute lymphoblastic leukemia antigen (CALLA Antigen), an important marker in the diagnosis of human acute lymphocytic leukemia. There is no relationship with CALLA PLANT.
Serine Endopeptidases
Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.
Thiorphan
A potent inhibitor of membrane metalloendopeptidase (ENKEPHALINASE). Thiorphan potentiates morphine-induced ANALGESIA and attenuates naloxone-precipitated withdrawal symptoms.
PHEX Phosphate Regulating Neutral Endopeptidase
A membrane-bound metalloendopeptidase that may play a role in the degradation or activation of a variety of PEPTIDE HORMONES and INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS. Genetic mutations that result in loss of function of this protein are a cause of HYPOPHOSPHATEMIC RICKETS, X-LINKED DOMINANT.
Protease Inhibitors
Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).
Cysteine Proteases
A subclass of peptide hydrolases that depend on a CYSTEINE residue for their activity.
Metalloendopeptidases
ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.
Cysteine Proteinase Inhibitors
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
Cysteine Dioxygenase
An enzyme that catalyzes the conversion of L-CYSTEINE to 3-sulfinoalanine (3-sulfino-L-alanine) in the CYSTEINE metabolism and TAURINE and hypotaurine metabolic pathways.
Substrate Specificity
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Cysteine Synthase
An enzyme that catalyzes the biosynthesis of cysteine in microorganisms and plants from O-acetyl-L-serine and hydrogen sulfide. This enzyme was formerly listed as EC 4.2.99.8.
Glycopeptides
Proteins which contain carbohydrate groups attached covalently to the polypeptide chain. The protein moiety is the predominant group with the carbohydrate making up only a small percentage of the total weight.
Disulfides
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Neurotensin
A biologically active tridecapeptide isolated from the hypothalamus. It has been shown to induce hypotension in the rat, to stimulate contraction of guinea pig ileum and rat uterus, and to cause relaxation of rat duodenum. There is also evidence that it acts as both a peripheral and a central nervous system neurotransmitter.
Serine Proteinase Inhibitors
Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.
Hydrolysis
The process of cleaving a chemical compound by the addition of a molecule of water.
Kinetics
The rate dynamics in chemical or physical systems.
Dipeptides
Peptides composed of two amino acid units.
Lysostaphin
A 25-kDa peptidase produced by Staphylococcus simulans which cleaves a glycine-glcyine bond unique to an inter-peptide cross-bridge of the STAPHYLOCOCCUS AUREUS cell wall. EC 3.4.24.75.
Aspartic Acid Endopeptidases
A sub-subclass of endopeptidases that depend on an ASPARTIC ACID residue for their activity.
Cathepsins
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
Sulfhydryl Compounds
Compounds containing the -SH radical.
Base Sequence
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Chromatography, High Pressure Liquid
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.

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)

Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold...Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold...
Read Effects of abscisic acid treatment on the expression of cysteine proteinase gene and enzyme inhibitor during wheat cold adaptation, Russian Journal of Plant Physiology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
https://www.deepdyve.com/lp/springer_journal/effects-of-abscisic-acid-treatment-on-the-expression-of-cysteine-iqHw3KEtx7
Circadian and senescence-enhanced expression of a tobacco cysteine protease gene, Plant Molecular Biology | 10.1023/A...Circadian and senescence-enhanced expression of a tobacco cysteine protease gene, Plant Molecular Biology | 10.1023/A...
Read Circadian and senescence-enhanced expression of a tobacco cysteine protease gene, Plant Molecular Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
https://www.deepdyve.com/lp/springer_journal/circadian-and-senescence-enhanced-expression-of-a-tobacco-cysteine-p8fm11lyZg
Substrate specificity and rational design of peptidomimetic inhibitors for SARS coronavirus main protease | HKMJSubstrate specificity and rational design of peptidomimetic inhibitors for SARS coronavirus main protease | HKMJ
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 ...
http://www.hkmj.org/abstracts/v20n4s4/18.htm
Plus itPlus it
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 ...
http://cancerres.aacrjournals.org/content/58/19/4342
CNF1/YfiH-like putative cysteine hydrolases superfamily
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.
http://supfam.org/SUPERFAMILY/cgi-bin/scop.cgi?ipid=SSF64438
CNF1/YfiH-like putative cysteine hydrolases superfamilyCNF1/YfiH-like putative cysteine hydrolases superfamily
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.
http://supfam.mrc-lmb.cam.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=64438
Mindfire PlatformMindfire Platform
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 ...
https://platform.mindfire.global/quests/determine-the-corona-virus-susceptibilities
Browsing ICR Divisions by subject Cysteine Endopeptidases
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 ...
https://repository.icr.ac.uk/handle/internal/1/browse?value=Cysteine+Endopeptidases&type=subject
BDNF inhibits neurodegenerative disease-associated asparaginyl endopeptidase activity via phosphorylation by AKT - Vector...BDNF inhibits neurodegenerative disease-associated asparaginyl endopeptidase activity via phosphorylation by AKT - Vector...
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.
https://www.vectorbiolabs.com/citation/bdnf-inhibits-neurodegenerative-disease-associated-asparaginyl-endopeptidase-activity-via-phosphorylation-by-akt/
Activity-based Probes That Target Diverse Cysteine Protease Families - PubMedActivity-based Probes That Target Diverse Cysteine Protease Families - PubMed
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 …
https://pubmed.ncbi.nlm.nih.gov/16407991/
Biochemical characterization of recombinant Avihepatovirus 3C protease and its localization | Virology Journal | Full TextBiochemical characterization of recombinant Avihepatovirus 3C protease and its localization | Virology Journal | Full Text
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
https://virologyj.biomedcentral.com/articles/10.1186/s12985-019-1155-3/figures/3
Characterization of legumain<...Characterization of legumain<...
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 ...
https://research.nu.edu.kz/en/publications/characterization-of-legumain
Expression of sweet potato asparaginyl endopeptidase caused altered phenotypic characteristics in transgenic Arabidopsis<...
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 ...
https://tmu.pure.elsevier.com/en/publications/expression-of-sweet-potato-asparaginyl-endopeptidase-caused-alter
The dissemination of C10 cysteine protease genes in Bacteroides fragilis by mobile genetic elements | BMC Microbiology | Full...The dissemination of C10 cysteine protease genes in Bacteroides fragilis by mobile genetic elements | BMC Microbiology | Full...
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
https://bmcmicrobiol.biomedcentral.com/articles/10.1186/1471-2180-10-122/tables/2
Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease...Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease...
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 ...
https://www.pnas.org/content/90/16/7676?ijkey=16b1e9d2e4b7d937fd4cf039adcfc8ef5295d2c9&keytype2=tf_ipsecsha
Null mutants for the lmcpa cysteine proteinase gene in Leishmania mexicana - Lancaster EPrintsNull mutants for the lmcpa cysteine proteinase gene in Leishmania mexicana - Lancaster EPrints
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, ...
http://eprints.lancs.ac.uk/56057/
Papain-like cysteine proteinase zone (PCP-zone) and PCP structural catalytic core (PCP-SCC) of enzymes with cysteine proteinase...Papain-like cysteine proteinase zone (PCP-zone) and PCP structural catalytic core (PCP-SCC) of enzymes with cysteine proteinase...
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. ...
https://research.abo.fi/sv/publications/papain-like-cysteine-proteinase-zone-pcp-zone-and-pcp-structural-/fingerprints/
Proteasome activator complex subunit 3Proteasome activator complex subunit 3
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 ...
https://pharos.nih.gov/idg/targets/P61289
Rapid amplification of cDNA end of metallothion in gene during necrosis of plant cells from morinda citrifolia - UNIMAS...Rapid amplification of cDNA end of metallothion in gene during necrosis of plant cells from morinda citrifolia - UNIMAS...
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 ...
https://ir.unimas.my/id/eprint/7670/
The substrate specificity of cruzipain 2, a cysteine protease isoform from Trypanosoma cruzi
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 ...
http://repositorio.unifesp.br/handle/11600/28927
PSME3 - WikipediaPSME3 - Wikipedia
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 ...
https://en.wikipedia.org/wiki/PSME3
26S proteasome non-ATPase regulatory subunit 526S proteasome non-ATPase regulatory subunit 5
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 ...
https://pharos.nih.gov/idg/targets/Q16401
Cysteine protease - WikipediaCysteine protease - Wikipedia
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, ...
https://en.wikipedia.org/wiki/Cysteine_protease
Immunoproteasome subunit LMP2 expression is deregulated in Sjögrens syndrome but not in other autoimmune disordersImmunoproteasome subunit LMP2 expression is deregulated in Sjögrens syndrome but not in other autoimmune disorders
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 ...
https://epub.ub.uni-muenchen.de/15009/
IJMS | Free Full-Text | Computational Study on Substrate Specificity of a Novel Cysteine Protease 1 Precursor from Zea mays |...
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
https://0-www-mdpi-com.brum.beds.ac.uk/1422-0067/15/6/10459/htm
Coronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs | ScienceCoronavirus Main Proteinase (3CLpro) Structure: Basis for Design of Anti-SARS Drugs | Science
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 ...
https://science.sciencemag.org/content/300/5626/1763
PSMC5 - Gemini GenomicsPSMC5 - Gemini Genomics
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 ...
https://gemini-genomics.com/psmc5/
Psmb11 - Proteasome subunit beta type-11 precursor - Mus musculus (Mouse) - Psmb11 gene & proteinPsmb11 - Proteasome subunit beta type-11 precursor - Mus musculus (Mouse) - Psmb11 gene & protein
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.
http://www.uniprot.org/uniprot/Q8BG41
PSMA2 proteasome 20S subunit alpha 2 [Homo sapiens (human)] - Gene - NCBIPSMA2 proteasome 20S subunit alpha 2 [Homo sapiens (human)] - Gene - NCBI
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 ...
https://www.ncbi.nlm.nih.gov/gene/5683
RCSB PDB - 2GT8: Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each...RCSB PDB - 2GT8: Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each...
2GT8: Crystal structure of SARS coronavirus main peptidase (with an additional Ala at the N-terminus of each protomer) in the space group P43212
https://www.rcsb.org/structure/2GT8
Caspase 3 (Apopain or Cysteine Protease CPP32 or Protein Yama or SREBP Cleavage Activity 1 or CASP3 or EC 3.4.22.56) - Pipeline...Caspase 3 (Apopain or Cysteine Protease CPP32 or Protein Yama or SREBP Cleavage Activity 1 or CASP3 or EC 3.4.22.56) - Pipeline...
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
https://www.researchmoz.us/caspase-3-apopain-or-cysteine-protease-cpp32-or-protein-yama-or-srebp-cleavage-activity-1-or-casp3-or-ec-342256-pipeline-review-h1-2017-report.html
PAD1 - Proteasome subunit alpha type-7-A - Arabidopsis thaliana (Mouse-ear cress) - PAD1 gene & proteinPAD1 - Proteasome subunit alpha type-7-A - Arabidopsis thaliana (Mouse-ear cress) - PAD1 gene & protein
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.
http://www.uniprot.org/uniprot/P30186
Agronomy | Free Full-Text | The Cysteine Protease-Cysteine Protease Inhibitor System Explored in Soybean Nodule Development |...Agronomy | Free Full-Text | The Cysteine Protease-Cysteine Protease Inhibitor System Explored in Soybean Nodule Development |...
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
http://www.mdpi.com/2073-4395/3/3/550/notes
PSMA3 antibodies | AntibodypediaPSMA3 antibodies | Antibodypedia
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] ...
https://www.antibodypedia.com/gene/80/PSMA3
Search Results | Biochemical Journal | Portland PressSearch Results | Biochemical Journal | Portland Press
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 ...
https://portlandpress.com/biochemj/search-results?f_Authors=Graciela+FUERTES
Solyc11g069150.1.1 protein (Solanum lycopersicum) - STRING network viewSolyc11g069150.1.1 protein (Solanum lycopersicum) - STRING network view
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 ...
https://string-db.org/cgi/network.pl?identifier=4081.Solyc11g069150.1.1
PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in...PanDDA analysis group deposition SARS-CoV-2 main protease fragment screen -- Crystal Structure of SARS-CoV-2 main protease in...
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 ...
https://3dprint.nih.gov/discover/3DPX-014480
Plus itPlus it
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 ...
http://cancerres.aacrjournals.org/content/early/2011/11/15/0008-5472.CAN-10-1883
Strukturelle und biochemische Analyse der 20S Proteasom-Subtypen aus humanen ZellenStrukturelle und biochemische Analyse der 20S Proteasom-Subtypen aus humanen Zellen
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 ...
https://edoc.hu-berlin.de/handle/18452/15956?C=M
Base-CP proteasome can serve as a platform for stepwise lid formation<...
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 ...
https://experts.syr.edu/en/publications/base-cp-proteasome-can-serve-as-a-platform-for-stepwise-lid-forma
In-Silico Identification of Potent Inhibitors of COVID-19 Main Protease (Mpro) and Angiotensin Converting Enzyme 2 (ACE2) from...In-Silico Identification of Potent Inhibitors of COVID-19 Main Protease (Mpro) and Angiotensin Converting Enzyme 2 (ACE2) from...
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
https://chemrxiv.org/articles/preprint/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/12181404/1
Publications - Luks research groupPublications - Luks research group
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…
https://louisluklab.org/publications/
PA700 proteasome activator Summary Report | CureHunterPA700 proteasome activator Summary Report | CureHunter
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
http://www.curehunter.com/public/keywordSummaryC085834-PA700-proteasome-activator.do
Dynamical properties of enzyme-substrate complexes disclose substrate specificity of the SARS-CoV-2 main protease as...Dynamical properties of enzyme-substrate complexes disclose substrate specificity of the SARS-CoV-2 main protease as...
Dynamical properties of enzyme-substrate complexes disclose substrate specificity of the SARS-CoV-2 main protease as characterized by the electron density ...
https://lcc.chem.msu.ru/publication/nemukhin-2020-dynamical-318876724/
Relationship of the surface export of SDH and SpeB secr | Open-iRelationship of the surface export of SDH and SpeB secr | Open-i
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
https://openi.nlm.nih.gov/detailedresult.php?img=PMC3104492_mbo0031111190005&req=4
RCSB PDB - Launch Viewer for 4EKFRCSB PDB - Launch Viewer for 4EKF
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.
http://www.rcsb.org/pdb/explore/viewerLaunch.do?viewerType=LX&structureId=4EKF
Evidence for a role of immunoproteasomes in regulating cardiac muscle mass in diabetic mice - Fingerprint - Johns Hopkins...
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. ...
https://jhu.pure.elsevier.com/en/publications/evidence-for-a-role-of-immunoproteasomes-in-regulating-cardiac-mu-4/fingerprints/
Browse WishlistBrowse Wishlist
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 ...
https://www.celltechgen.com/product/caspase-3-polyclonal-antibody-3/
Proteases/ProteasomeProteases/Proteasome
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. ...
https://www.targetmol.com/pathway/Proteases-Proteasome
Switch to Europe/Worldwide website
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…
https://www.acris-antibodies.com/target/psme2-antibody-reg-beta-antibody.htm?ab_host=Rabbit
1pau.1 | SWISS-MODEL Template Library
SWISS-MODEL Template Library (SMTL) entry for 1pau.1. Crystal structure of the complex of apopain with the tetrapeptide aldehyde inhibitor AC-DEVD-CHO
https://swissmodel.expasy.org/templates/1pau.1
SCOP: Superfamily: Cysteine proteinases
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- ...
http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.e.d.b.html
16. Use Of SiliaBond® Cysteine<...16. Use Of SiliaBond® Cysteine<...
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.
https://www.silicycle.com/resource-center/applications-library/purification/metal-removal/16-use-of-siliabond-cysteine
Peptidase 1 (mite)Peptidase 1 (mite)
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 ...
https://en.wikipedia.org/wiki/Peptidase_1_(mite)
Cathepsin L2Cathepsin L2
The protein is a human cysteine cathepsin, a lysosomal cysteine protease with endopeptidase activity. The protein is a member ... a lysosomal cysteine protease with endopeptidase activity. It may play an important role in corneal physiology. This gene is ... 2005). "The human cysteine protease cathepsin V can compensate for murine cathepsin L in mouse epidermis and hair follicles". ... Santamaría I, Velasco G, Cazorla M, Fueyo A, Campo E, López-Otín C (April 1998). "Cathepsin L2, a novel human cysteine ...
https://en.wikipedia.org/wiki/Cathepsin_L2
NepenthesinNepenthesin
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 ...
https://en.wikipedia.org/wiki/Nepenthesin
Asparagine endopeptidaseAsparagine endopeptidase
... 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) ...
https://en.wikipedia.org/wiki/Asparagine_endopeptidase
Mountain papayaMountain papaya
... it contains a cysteine endopeptidase mixture especially present in immature fruits that is used commercially by the ...
https://en.wikipedia.org/wiki/Mountain_papaya
LGMNLGMN
... 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 ...
https://en.wikipedia.org/wiki/LGMN
RAD21RAD21
... 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 ...
https://en.wikipedia.org/wiki/RAD21
DISC1DISC1
... is also known to play a role in axon regeneration and has an additional DISC1-modulated function as a cysteine endopeptidase. ...
https://en.wikipedia.org/wiki/DISC1
Cathepsin XCathepsin X
Shows weak endopeptidase activity Cathepsin X is a cysteine cathepsin, a lysosomal cysteine peptidase of family C1 (papain ... 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, ...
https://en.wikipedia.org/wiki/Cathepsin_X
Glutamyl endopeptidase IGlutamyl endopeptidase I
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 ...
https://en.wikipedia.org/wiki/Glutamyl_endopeptidase_I
Glutamyl endopeptidase GluV8Glutamyl endopeptidase GluV8
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 ...
https://en.wikipedia.org/wiki/Glutamyl_endopeptidase_GluV8
FicainFicain
... before the terminology was restricted to a specific cysteine endopeptidase enzyme from a specific species. Cysteine ... Cysteine endopeptidases with similar properties known generically as ficins are present in other members of the genus Ficus, ... Ficain was originally called ficin, and ficin was originally a mixture of closely related cysteine endopeptidases produced from ... This, however, is not a cysteine protease, but a serine protease. The crude, unrefined latex of F. insipida is also sold in ...
https://en.wikipedia.org/wiki/Ficain
List of MeSH codes (D08)List of MeSH codes (D08)
... 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 ...
https://en.wikipedia.org/wiki/List_of_MeSH_codes_(D08)
Cysteine proteaseCysteine protease
The MEROPS online database for peptidases and their inhibitors: Cysteine Peptidases Cysteine+endopeptidases at the US National ... In fact, the latex of dozens of different plant families are known to contain cysteine proteases. Cysteine proteases are used ... Plant cysteine proteases isolated from these plants have been found to have high proteolytic activities that are known to ... Cysteine proteases are used as feed additives for livestock to improve the digestibility of proteins and amino acids. Protease ...
https://en.wikipedia.org/wiki/Cysteine_protease
AdenainAdenain
This cysteine endopeptidase is encoded by adenoviruses. Webster A, Hay RT, Kemp G (January 1993). "The adenovirus protease is ...
https://en.wikipedia.org/wiki/Adenain
TEV proteaseTEV protease
... (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 ...
https://en.wikipedia.org/wiki/TEV_protease
Coeliac diseaseCoeliac disease
... prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer peptide ...
https://en.wikipedia.org/wiki/Coeliac_disease
KexinKexin
... 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 ...
https://en.wikipedia.org/wiki/Kexin
Gingipain RGingipain R
This enzyme is secreted cysteine endopeptidase from the bacterium Porphyromonas gingivalis. Gingipain Gingipain K Chen Z, ... arginine-specific cysteine protease, arginine-specific gingipain, arginine-specific gingivain, RGP-1, RGP) is an enzyme. This ... Potempa J, Polanowski A, Wikstrom M, Travis J (September 1992). "Purification and characterization of a 50-kDa cysteine ... a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase ...
https://en.wikipedia.org/wiki/Gingipain_R
Glycyl endopeptidaseGlycyl endopeptidase
Buttle DJ, Kembhavi AA, Sharp SL, Shute RE, Rich DH, Barrett AJ (July 1989). "Affinity purification of the novel cysteine ... Glycyl+endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.22). ... Glycyl endopeptidase (EC 3.4.22.25, papaya peptidase B, papaya proteinase IV, glycine-specific proteinase, chymopapain, Papaya ...
https://en.wikipedia.org/wiki/Glycyl_endopeptidase
CHAP domainCHAP domain
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 ...
https://en.wikipedia.org/wiki/CHAP_domain
Cathepsin ZCathepsin Z
It is a member of the cysteine cathepsin family of cysteine proteases, which has 11 members. As one of the 11 cathepsins, ... It is an exopeptidase with strict carboxypeptidase activity, while most other cathepsins are endopeptidases. Cathepsin Z has an ... a cysteine protease with the proregion covalently linked to the active site cysteine". Journal of Molecular Biology. 295 (4): ... Santamaría I, Velasco G, Pendás AM, Fueyo A, López-Otín C (July 1998). "Cathepsin Z, a novel human cysteine proteinase with a ...
https://en.wikipedia.org/wiki/Cathepsin_Z
Ste24 endopeptidaseSte24 endopeptidase
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 at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 3.4.24). ... Ste24 endopeptidase (EC 3.4.24.84) is an enzyme. This enzyme catalyses the following chemical reaction The peptide bond ...
https://en.wikipedia.org/wiki/Ste24_endopeptidase
Endopeptidase inhibitorEndopeptidase inhibitor
... 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 ...
https://en.wikipedia.org/wiki/Endopeptidase_inhibitor
CalicivirinCalicivirin
... 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. ...
https://en.wikipedia.org/wiki/Calicivirin
MetalloproteinaseMetalloproteinase
... cysteine; G, glutamic acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine peptidases ... These endopeptidases include CAAX prenyl protease 1, which proteolytically removes the C-terminal three residues of ... There are two subgroups of metalloproteinases: Exopeptidases, metalloexopeptidases (EC number: 3.4.17). Endopeptidases, ...
https://en.wikipedia.org/wiki/Metalloproteinase
Calpain-2Calpain-2
This enzyme catalyses the following chemical reaction Broad endopeptidase specificity This enzyme belongs to the peptidase ... is an intracellular heterodimeric calcium-activated cysteine protease. ...
https://en.wikipedia.org/wiki/Calpain-2
Atrolysin AAtrolysin A
This endopeptidase has a length of 419 amino acid residues. The metalloproteinase disintegrin-like domain and the cysteine-rich ... The cysteine-rich domain was shown to have two sequences that cause an interaction which prevents alpha-2/beta-1 integrin ... Research suggests that the RSECD cysteine residue at positions 272-276 must be involved in a disulfide bond for the enzyme to ... This suggests that there may be an interaction between the disintegrin-like domain, and cysteine-rich domain of atrolysin A and ...
https://en.wikipedia.org/wiki/Atrolysin_A
Achromobacter lyticusAchromobacter lyticus
The enzyme lysyl endopeptidase was isolated from A. lyticus. Uniprot Straininfo of Achromobacter lyticus Uniprot Methods in ... 244 Proteolytic Enzymes: Serine and Cysteine Peptidases Serogrouping Single Colonies of Beta-hemolytic Streptococci with ...
https://en.wikipedia.org/wiki/Achromobacter_lyticus
Papain-like proteasePapain-like protease
... s (or papain-like (cysteine) peptidases; abbreviated PLP or PLCP) are a large protein family of cysteine ... Papain-like proteases are usually endopeptidases, but some members of the group are also, or even exclusively, exopeptidases. ... which includes cysteine, serine, and aspartic proteases). In humans, there are 11 cysteine cathepsins: B, C, F, H, K, L, O, S, ... Cysteine cathepsins are also part of the normal life cycle of the unicellular parasite Leishmania, where they function as ...
https://en.wikipedia.org/wiki/Papain-like_protease
ATG4DATG4D
Mariño G, Uría JA, Puente XS, Quesada V, Bordallo J, López-Otín C (February 2003). "Human autophagins, a family of cysteine ... This gene belongs to the autophagy-related protein 4 (Atg4) family of C54 endopeptidases. Members of this family encode ... "Entrez Gene: Autophagy related 4D, cysteine peptidase". Betin VM, MacVicar TD, Parsons SF, Anstee DJ, Lane JD (April 2012). "A ... The human ATG4D gene encodes the protein Autophagy related 4D, cysteine peptidase. Autophagy is the process by which endogenous ...
https://en.wikipedia.org/wiki/ATG4D
Plant matrix metalloproteinasePlant matrix metalloproteinase
For example, SMEP1 is said to have a free cysteine at position 94, a non-homologous insert from V103 to S121, a free sulfhydryl ... Matrix metalloproteinases (MMPs) are zinc endopeptidases, commonly called metzincins. MMP enzymes represent an ancient family ... Plant MMPs show structural similarity to MMPs found in mammals, such as the presence of an auto-regulatory cysteine switch ...
https://en.wikipedia.org/wiki/Plant_matrix_metalloproteinase
Picornain 3CPicornain 3C
... are cysteine proteases related by amino acid sequence to trypsin-like serine proteases. Picornain 3C is encoded by ... Picornain 3C's endopeptidase activity is primarily responsible for the catalytic process of selectively cleaving Gln-Gly bonds ... Hepatitis A 3C proteinase is a member of the cysteine proteases that are responsible for the infectivity and maturation of HAV ... Both 2A(pro) and 3C(pro) induce caspase-8-mediated by activation of caspase-3. Caspase stands for cysteine-aspartic acid ...
https://en.wikipedia.org/wiki/Picornain_3C
Proteases in angiogenesisProteases in angiogenesis
In humans, the group of cathepsin cysteine proteases or cysteine cathepsins comprises 11 family members, cathepsins B, C, F, H ... MMPs are a large multigene family of zinc-dependent endopeptidases. The collective MMP family is capable of degrading all known ... 2004). "Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis". Cancer ... They include serine, aspartic, and cysteine-type proteases. A highly characterized example of the serine protease family is the ...
https://en.wikipedia.org/wiki/Proteases_in_angiogenesis
Death regulator Nedd2-like caspaseDeath regulator Nedd2-like caspase
It is defined as a cysteine protease (or thiol protease), which means that a nucleophilic cysteine thiol forms a catalytic ... The main function of this kind of endopeptidases is to catalyze the hydrolysis of peptide bonds in order to cleave proteins ... It belongs to the cysteine-aspartic proteases family, as it is a protease enzyme that takes part in programmed cell death ... "FlyBase Gene Report: Dmel\Dronc". Kumar S, Lavin MF (July 1996). "The ICE family of cysteine proteases as effectors of cell ...
https://en.wikipedia.org/wiki/Death_regulator_Nedd2-like_caspase
OxytocinOxytocin
... 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): 1119-1125. doi:10.1016/0196-9781(91)90068-z. PMID 1800950. S2CID ... its C-terminus has been converted to a primary amide and a disulfide bridge joins the cysteine moieties. Oxytocin has a ...
https://en.wikipedia.org/wiki/Oxytocin
OsteoclastOsteoclast
Cathepsin K is a collagenolytic papain-like cysteine protease that is mainly expressed in osteoclasts, and is secreted into the ... The matrix metalloproteinases (MMPs) comprise a family of more than 20 zinc-dependent endopeptidases. The role of matrix ... The function of these cysteine and aspartic proteases is generally unknown within bone, and they are expressed at much lower ...
https://en.wikipedia.org/wiki/Osteoclast
Protease inhibitor (biology)Protease inhibitor (biology)
This domain is also found, in one or more copies, in a variety of cysteine peptidase inhibitors such as salarin. The ... This family includes PinA, which inhibits the endopeptidase La. It binds to the La homotetramer but does not interfere with the ... It has no similarity to any other known cysteine proteinase inhibitors but bears some similarity to a lectin-like family of ... Brzin J, Rogelj B, Popovic T, Strukelj B, Ritonja A (June 2000). "Clitocypin, a new type of cysteine proteinase inhibitor from ...
https://en.wikipedia.org/wiki/Protease_inhibitor_(biology)
MMP7MMP7
Cysteine residues bind to the catalytic zinc keeping the protein latent. The dissociation of cysteine -Zinc coordination starts ... MMP7 is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. ... The prodoamin of MMP7 contains an approximately 9 kD highly conserved "cysteine switch" PRCGXPD sequence near the C-terminal ...
https://en.wikipedia.org/wiki/MMP7
Active siteActive site
The NADPH is involved in the generation of FADH-. In the active site, there are two cysteine residues besides the FAD cofactor ... 137-9 Chymotrypsin is a serine endopeptidase that is present in pancreatic juice and helps the hydrolysis of proteins and ... Next the adjacent S− group attack disulphide bond in cysteine-SG complex and release the second SG− anion. It receives one ... Many enzymes including serine protease, cysteine protease, protein kinase and phosphatase evolved to form transient covalent ...
https://en.wikipedia.org/wiki/Active_site
Peptidoglycan recognition protein 1Peptidoglycan recognition protein 1
These cell-separating endopeptidases likely expose PGLYRP1-binding muramyl peptides, as shown by co-localization of PGLYRP1 and ... PGLYRP1 has three pairs of conserved cysteines, which form three disulfide bonds at positions 9 and 133, 25 and 70, and 46 and ... This localization is necessary for the bacterial killing, because mutants that lack LytE and LytF endopeptidases and do not ... created by bacterial peptidoglycan-lytic endopeptidases, LytE and LytF in B. subtilis, which separate the daughter cells after ...
https://en.wikipedia.org/wiki/Peptidoglycan_recognition_protein_1
Metalloprotease inhibitorMetalloprotease inhibitor
They all contain twelve cysteine residues that form six disulfide bonds. These bonds are critical for the conformation of the N ... MMPs belong to a family of zinc-dependent neutral endopeptidases. These enzymes have the ability to break down connective ... reversion-inducing cysteine-rich protein with Kazal motifs (RECK) and tissue factor pathway inhibitor (TFPI-2)). They might ...
https://en.wikipedia.org/wiki/Metalloprotease_inhibitor
Atrial natriuretic peptideAtrial natriuretic peptide
The ring is formed by a disulfide bond between two cysteine residues at positions 7 and 23. ANP is closely related to BNP ( ... Neutral endopeptidase (NEP) also known as neprilysin is the enzyme that metabolizes natriuretic peptides. Several inhibitors of ... Modulation of the effects of ANP is achieved through gradual degradation of the peptide by the enzyme neutral endopeptidase ( ...
https://en.wikipedia.org/wiki/Atrial_natriuretic_peptide
Protein metabolismProtein metabolism
Endopeptidases are enzymes that add water to an internal peptide bond in a peptide chain and break that bond. Three common ... Disulfide bond formation is the creation of disulfide bridges (covalent bonds) between two cysteine amino acids in a chain ... endopeptidases that come from the pancreas are pepsin, trypsin, and chymotrypsin. Chymotrypsin performs a hydrolysis reaction ...
https://en.wikipedia.org/wiki/Protein_metabolism
Stichodactyla toxinStichodactyla toxin
"Crystal structure of the cysteine-rich secretory protein stecrisp reveals that the cysteine-rich domain has a K+ channel ... and likely functions as an endopeptidase. MMP-23's ShK domain lies immediately after the catalytic domain and is connected to ... More distantly related are Cysteine-rich secretory proteins (CRISPs), which contain a ShK-like 'Cystine-rich domain' as well as ... Koppers AJ, Reddy T, O'Bryan MK (January 2011). "The role of cysteine-rich secretory proteins in male fertility". Asian Journal ...
https://en.wikipedia.org/wiki/Stichodactyla_toxin
Asparagine peptide lyaseAsparagine peptide lyase
The N-terminal residue of the intein domain must be a serine, threonine or cysteine, and it attacks its preceding peptide bond ... Family N2: Includes tetraviruses endopeptidases. The known autolytic cleavage is from the C-terminus of the coat protein. The ... The first residue of the second portion of the extein must be a serine, threonine or cysteine as well, and this second ... Reddy, A., Schneemann, A. & Johnson, J.E. Nodavirus endopeptidase. In Handbook of Proteolytic Enzymes, 2 edn (Barrett, A.J., ...
https://en.wikipedia.org/wiki/Asparagine_peptide_lyase
ADAM (protein)ADAM (protein)
"ADAM, cysteine-rich (IPR006586)". InterPro. Retrieved 18 February 2016. Edwards DR, Handsley MM, Pennington CJ (October 2008 ... ". "Entrez Gene: ADAM9 ADAM metallopeptidase domain 9 (meltrin gamma)". "Entry of ADAM10 endopeptidase (EC-Number 3.4.24.81 ... The terms adamalysin and MDC family (metalloproteinase-like, disintegrin-like, cysteine rich) have been used to refer to this ... a cysteine-rich, an epidermal-growth factor like and a transmembrane domain, as well as a C-terminal cytoplasmic tail. ...
https://en.wikipedia.org/wiki/ADAM_(protein)
KOPS.Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defenseKOPS.Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense
Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense. * Home ... Plant PCD is effected by a unique group of papain-type cysteine endopeptidases (CysEP) with a C-terminal KDEL endoplasmic ... Plant PCD is effected by a unique group of papain-type cysteine endopeptidases (CysEP) with a C-terminal KDEL endoplasmic ... Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense. Type of ...
https://kops.uni-konstanz.de/handle/123456789/38159
GO:0004198calcium-dependent cysteine-type endopeptidase activity - SlorthGO:0004198calcium-dependent cysteine-type endopeptidase activity - Slorth
calcium-dependent cysteine-type endopeptidase activity. Associated Genes. Gene Name Gene ID Description ...
http://rails.biochem.susx.ac.uk/gos/596
Systematic changes in gene expression in postmortem human brains associated with tissue pH and terminal medical conditionsSystematic changes in gene expression in postmortem human brains associated with tissue pH and terminal medical conditions
Cysteine Endopeptidases * Proteasome Endopeptidase Complex Grant support * MH60398/MH/NIMH NIH HHS/United States ...
https://pubmed.ncbi.nlm.nih.gov/14734628/
KNG1 kininogen 1 [Homo sapiens (human)] - Gene - NCBIKNG1 kininogen 1 [Homo sapiens (human)] - Gene - NCBI
enables cysteine-type endopeptidase inhibitor activity IBA Inferred from Biological aspect of Ancestor. more info ... enables cysteine-type endopeptidase inhibitor activity IDA Inferred from Direct Assay. more info ... enables endopeptidase inhibitor activity IBA Inferred from Biological aspect of Ancestor. more info ... involved_in negative regulation of endopeptidase activity IBA Inferred from Biological aspect of Ancestor. more info ...
https://www.ncbi.nlm.nih.gov/gene/3827
Trypanosoma cruzi: chemotherapeutic effects of clomipramine in mice infected with an isolate obtained from an endemic area. |...Trypanosoma cruzi: chemotherapeutic effects of clomipramine in mice infected with an isolate obtained from an endemic area. |...
Cysteine Endopeptidases. *cruzipain. *Clomipramine. Topics. *Animals. *Antibodies, Protozoan (blood) *Antidepressive Agents, ...
https://www.curehunter.com/public/pubmed16085036.do
Gene Ontology ClassificationsGene Ontology Classifications
Predicted to enable cysteine-type endopeptidase inhibitor activity. Predicted to act upstream of or within negative regulation ...
http://www.informatics.jax.org/go/marker/MGI:107161
MeSH BrowserMeSH Browser
Cysteine Proteases [D08.811.277.656.262] * Cysteine Endopeptidases [D08.811.277.656.262.500] * Bromelains [D08.811.277.656. ... Gingipain Cysteine Endopeptidases Preferred Term Term UI T000955113. Date04/10/2019. LexicalTag NON. ThesaurusID NLM (2020). ... Gingipain Cysteine Endopeptidases Preferred Concept UI. M000648543. Registry Number. 0. Related Numbers. 3HJ2M2X2UM. EC 3.4.22 ... Gingipain Cysteine Endopeptidases. Tree Number(s). D08.811.277.656.262.500.468. Unique ID. D000080867. RDF Unique Identifier. ...
https://meshb.nlm.nih.gov/record/ui?ui=D000080867
Evaluation of the Efficacy and Safety of ALV003 in Symptomatic in Celiac Disease Patients - Full Text View - ClinicalTrials.govEvaluation of the Efficacy and Safety of ALV003 in Symptomatic in Celiac Disease Patients - Full Text View - ClinicalTrials.gov
ALV003 is an orally administered mixture of two enzymes (cysteine endoprotease B-isoform 2 and prolyl endopeptidase) ...
https://clinicaltrials.gov/ct2/show/NCT01917630?term=alv003-1221&rank=1
TCDB » SEARCHTCDB » SEARCH
GO:0004197 F:cysteine-type endopeptidase activity GO:0005216 F:ion channel activity ...
https://tcdb.org/search/result.php?tc=1.A.53.1.5
CATH Superfamily 3.90.1170.50CATH Superfamily 3.90.1170.50
Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919 Any process that initiates the ... Activation of cysteine-type endopeptidase activity involved in apoptotic process GO:0006919 Any process that initiates the ... activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process. ... activity of the inactive enzyme cysteine-type endopeptidase in the context of an apoptotic process. ...
http://www.cathdb.info/version/v4_3_0/superfamily/3.90.1170.50/funfam/2/go
SMART: calpain III domain annotationSMART: calpain III domain annotation
Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... This group of cysteine peptidases belong to the MEROPS peptidase family C2 (calpain family, clan CA). A type example is calpain ... Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique ...
http://smart.embl-heidelberg.de/smart/do_annotation.pl?DOMAIN=calpain_III&BLAST=DUMMY
SMART: Pfam domain OTUSMART: Pfam domain OTU
Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They ... A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a ... Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine ... Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. ...
https://smart.embl.de/smart/do_annotation.pl?DOMAIN=Pfam:OTU&START=70&END=185&E_VALUE=3.6e-12&TYPE=PFAM&BLAST=PGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIRQREDFEPFVEDDIPFEKHVASLSKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTDKGSTRELHIAYRYGEHYDSV
BIRC7 Protein - Creative BioMart
... cysteine-type endopeptidase inhibitor activity, cysteine-type endopeptidase inhibitor activity involved in apoptotic process, ... cysteine-type endopeptidase inhibitor activity. Cstb; CTLA2B; CST6; PTTG1; CST7; KNG1; CST9L; NGP; CST3; WFDC2. ... cysteine-type endopeptidase inhibitor activity involved in apoptotic process. TNFSF14; RPS6KA1; VIL1; RPS6KA3; BIRC5; AVP; ...
https://www.creativebiomart.net/symbolsearch_birc7.htm
歯学部門 - 研究成果 - 九州大学
Martin Witte - Research output - the University of Groningen research portalMartin Witte - Research output - the University of Groningen research portal
Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP ... Novel Aza Peptide Inhibitors and Active-Site Probes of Papain-Family Cysteine Proteases. Verhelst, S. H. L., Witte, M. D., ...
https://research.rug.nl/en/persons/martin-witte/publications/?ordering=publicationYearThenTitle&descending=false
Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch....Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch....
... showed partial homology with those of other cysteine proteinases of biological origin. This is the first paper to characterize ... A new cysteine protease named Nivulian-II has been purified from the latex of ,i,Euphorbia nivulia,/i, Buch.-Ham. The apparent ... S. R. Morcelle, S. A. Trejo, F. Canals, F. X. Aviles, and N. S. Priolo, "Funastrain c II: a cysteine endopeptidase purified ... with other cysteine endopeptidase isolated from the latex of rubber tree, Hevea brasiliensis Muell, Arg [19], and a member of ...
https://www.hindawi.com/journals/jaa/2013/569527/
Schmid, Markus - Regulation of Plant Growth & Development by the Environment - Umeå Plant Science Centre
article{schmid_cysteine_1998, title = {A cysteine endopeptidase with a {C}-terminal {KDEL} motif isolated from castor bean ... The cysteine endopeptidase from castor bean endosperm, which represents a senescing tissue, is homologous to cysteine ... The cysteine endopeptidase from castor bean endosperm, which represents a senescing tissue, is homologous to cysteine ... KDEL-tailed cysteine endopeptidases are unique in being able to digest the extensins that form the basic scaffold for cell wall ...
https://www.upsc.se/researchers/5841-schmid-markus-regulation-of-plant-growth-development-by-the-environment.html
OCA Atlas for 1A67
cysteine-type endopeptidase .... Primary reference. The structures of native phosphorylated chicken cystatin and of a ...
http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A67
2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE: Uses, Interactions, Mechanism of Action |...2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE: Uses, Interactions, Mechanism of Action |...
Cysteine-type endopeptidase activity. Gene Name. Not Available. Uniprot ID. P0C6U8. Uniprot Name. Replicase polyprotein 1a. ...
https://go.drugbank.com/drugs/DB07620
Genes | Free Full-Text | Impacts of the Type I Toxin-Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene ExpressionGenes | Free Full-Text | Impacts of the Type I Toxin-Antitoxin System, SprG1/SprF1, on Staphylococcus aureus Gene Expression
... glutamyl endopeptidase (SspA) and cysteine protease, staphopain B (SspB)), and cell membrane-bounded ATP synthase subunit α ( ... Interestingly, the only differentially expressed bona fide secretory proteins in SprG1-devoid strains were cysteine protease ...
https://www.mdpi.com/2073-4425/12/5/770/htm
Human T-cell leukemia virus type 1 Tax protein binds to assembled nuclear proteasomes and enhances their proteolytic activity. ...
Biological Transport, Cell Line, Cell Nucleus, Cysteine Endopeptidases, Gene Products, tax, Histocompatibility Antigens Class I ...
https://www.ndph.ox.ac.uk/publications/31965
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2019.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2016.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2011.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2007.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2017.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2020.bvsalud.org/I/rep_i2000.htm
DeCS - Changed termsDeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2015.bvsalud.org/I/rep_i2000.htm
DeCS - Changed terms
CYSTEINE PROTEINASES. CYSTEINE ENDOPEPTIDASES. DATAPHONE. MODEMS. DE LANGES SYNDROME. DE LANGE SYNDROME. ...
https://decs2010.bvsalud.org/I/rep_i2000.htm
ProteaseClans of cysteine peptidasesAsparaginyl endopeptidaseInhibitorASPARTIC ENDOPEPTIDASESResiduePorphyromonasProteinasesProteinHydrolasesSerineProteinsGingipainCatalyticCaspasesARGININETertiaryPlantFamilyFoldSimilarProteasesPeptidaseActivation of cysteine-type endopeptidase activityInhibitor activityCathepsinsProteinsInhibitorsPeptidasesActivityProteinAsparagineExtracellularMolecularAmino acidSpecificityStructurallyMutantsAcidGenesGroupComplexes
Protease7
  • Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch. (hindawi.com)
  • A new cysteine protease named Nivulian-II has been purified from the latex of Euphorbia nivulia Buch. (hindawi.com)
  • Additionally, we characterized the glycosylated cysteine protease called Nivulian-II of the latex of E. nivulia [ 5 ]. (hindawi.com)
  • This paper describes the biochemical characterization, of this cysteine like protease with respect to peptide fingerprinting and N-terminal amino acid sequencing. (hindawi.com)
  • Identification of a cysteine protease closely related to interleukin-1 beta-converting enzyme. (deathbase.org)
  • Using transfection experiments into mammalian cells, we demonstrate that TY has protease activity on its own precursor and that this activity is dependent on the presence of a cysteine residue at position 245. (deathbase.org)
  • Rabbit anti caspase-9 p10 antibody recognizes caspase-9, a member of the cysteine-aspartic acid protease family. (bio-rad-antibodies.com)
Clans of cysteine peptidases1
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (embl-heidelberg.de)
Asparaginyl endopeptidase1
  • Legumain/asparaginyl endopeptidase controls extracellular matrix remodeling through the degradation of fibronectin in mouse renal proximal tubular cells. (genebiosystems.com)
Inhibitor2
  • Predicted to enable cysteine-type endopeptidase inhibitor activity. (jax.org)
  • BIRC7 has several biochemical functions, for example, cysteine-type endopeptidase inhibitor activity, cysteine-type endopeptidase inhibitor activity involved in apoptotic process, enzyme binding. (creativebiomart.net)
ASPARTIC ENDOPEPTIDASES1
  • In this connection, we also propose the names of aspartic endopeptidases from the digestive fluids of relevant carnivorous plants. (carnivorousplants.org)
Residue5
  • A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. (embl-heidelberg.de)
  • 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. (embl-heidelberg.de)
  • 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. (embl-heidelberg.de)
  • Peptidases in which the nucleophile that attacks the scissile peptide bond is the sulfhydryl group of a cysteine residue are known as cysteine-type peptidase. (hindawi.com)
  • Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. (systemsbiology.net)
Porphyromonas1
  • Cysteine endoproteinases, from periodontal pathogen PORPHYROMONAS GINGIVALIS , acting as virulence factors associated with PERIODONTITIS . (nih.gov)
Proteinases1
  • The N-terminal sequence (DFPPNTCCCICC) showed partial homology with those of other cysteine proteinases of biological origin. (hindawi.com)
Protein1
  • it replaces the amino acid cysteine with a signal to stop protein production prematurely (written as Cys135Ter or C135X). (medlineplus.gov)
Hydrolases2
  • Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. (embl.de)
  • Hydrolases, Acting on peptide bonds (peptide hydrolases), Cysteine endopeptidases. (uma.es)
Serine2
  • Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. (embl.de)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (embl.de)
Proteins3
  • Plant cysteine proteases play a major role in the intracellular and extracellular process such as development and ripening of fruits, degradation of storage proteins in germinating seeds, activation of proteins, and degradation of defective proteins [ 3 ]. (hindawi.com)
  • Carnivorous plants are known to secrete various endopeptidases extracellularly to digest prey proteins. (carnivorousplants.org)
  • In a continuation of these studies, we have been attempting to characterize these and other endopeptidases secreted by carnivorous plants to digest prey proteins. (carnivorousplants.org)
Gingipain1
  • A novel lysine-specific cysteine proteinase, termed 'Lys-gingipain,' was purified from the culture supernatant of the Arg-gingipain-deficient mutant of P. gingivalis (KDP112) by a simple method including immunoaffinity chromatography. (elsevier.com)
Catalytic1
  • In this case, the conserved cysteine and aspartate in motif I and the histidine in motif IV could be the catalytic residues. (embl.de)
Caspases1
  • We further suggest that metacaspases and paracaspases, although sharing structural and mechanistic features with the metazoan caspases, form a distinct family of clan CD cysteine peptidases. (rupress.org)
ARGININE1
  • They are produced as pre-proproteins which mature into ARGININE and LYSINE specific endopeptidases. (nih.gov)
Tertiary1
  • Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. (embl-heidelberg.de)
Plant4
  • Plant PCD is effected by a unique group of papain-type cysteine endopeptidases (CysEP) with a C-terminal KDEL endoplasmic reticulum (ER) retention signal (KDEL CysEP). (uni-konstanz.de)
  • Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. (embl-heidelberg.de)
  • Plant cysteine proteases belong to a class which has been widely studied over the years. (hindawi.com)
  • Asparaginyl endopeptidases (AEP) are cysteine proteases found in mammalian and plant cells. (cardiff.ac.uk)
Family1
  • TY therefore represents a new member of the growing family of apoptosis-inducing ICE-related cysteine proteases. (deathbase.org)
Fold1
  • Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases. (embl.de)
Similar1
  • In the present report, we describe the occurrence of a similar cysteine endopeptidase in the digestive fluid of Drosera indica and propose the name "droserain" to this enzyme. (carnivorousplants.org)
Proteases10
  • The research group is particularly interested in cysteine proteases (legumain, cathepsins) and their roles in normal physiology and diseases (pathophysiology). (uio.no)
  • Main projects involve studying the interplay between and drug effects on cysteine proteases and their endogenous inhibitors (cystatins) in atherosclerosis, cancer and osteoporosis. (uio.no)
  • Development of an isotope-coded activity-based probe for the quantitative profiling of cysteine proteases. (ox.ac.uk)
  • Background Cystatins are inhibitors of cysteine proteases. (capecodmushroom.org)
  • Background The individual cathepsins B and L are cysteine proteases from the papain subfamily, which mainly work as endopeptidases within endolysosomal compartments. (capecodmushroom.org)
  • Cystatins make use of three structural components to interact and inhibit cysteine proteases, two loops alongside the N-terminal area. (capecodmushroom.org)
  • Cathepsin B, a member of the papain family of cysteine proteases, has also been called Cathepsin B1 and APP secretase. (immunochemistry.com)
  • Background The 11 human cysteine cathepsins are proteases primarily located in the endolysosomal compartment of all cells and within the exocytosis pathways of some secretory cell types. (perlierusa.com)
  • Interestingly cathepsin C, a strict aminopeptidase, and Ctsh are the only cysteine-cathepsins found in the secretory compartment of type II pneumocytes, and both proteases have been shown to be functionally redundant [15], [16]. (perlierusa.com)
  • In serine proteases, all three are arranged in a line on one side of the target protein chain, and in legumain, the cysteine and the histidine/asparagine attack the chain from opposite sides. (rcsb.org)
Peptidase5
  • A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. (embl.de)
  • Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad. (rostlab.org)
  • The active site features a novel Cys-His-His catalytic triad that appears to be a unique structural signature of this cysteine peptidase family. (rostlab.org)
  • The primary cysteine peptidase (CP) from can be cruzipain, a papain-like endopeptidase indicated like a 57-kDa proteins in every complete existence routine phases from the parasite, becoming more loaded in replicating forms and in the insect epimastigote stage especially. (alzheimers-conference.com)
  • RhoA is required for the apical junction formation of keratinocyte cell-cell adhesion, and serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. (thermofisher.com)
Activation of cysteine-type endopeptidase activity1
  • From NCBI Gene: Involved in activation of cysteine-type endopeptidase activity. (nih.gov)
Inhibitor activity1
  • Predicted to have cysteine-type endopeptidase inhibitor activity. (zfin.org)
Cathepsins4
  • The functional roles of legumain have mainly been associated with the presence in lysosomes where legumain is active and mediates processing of multiple proteins, such as the conversion of single to double chain forms of cysteine cathepsins. (uio.no)
  • For quantification of hemoglobin degradation, the tick gut draw out was preincubated for 10 min with 10 m E-64 and 1 m Aza-N-11a (12) to prevent undesired hydrolysis by cysteine cathepsins and asparaginyl endopeptidase. (barasertib.info)
  • Denotes an enlarged transcript in and and and and and and reporter FIGF in the Ctsh targeting construct a selective expression was detected in distinct alveolar cells in lungs of and in cultured human pneumocytes demonstrated processing of SP-B by cysteine cathepsins and identified Ctsh as the very likely candidate [14], [19]. (perlierusa.com)
  • 11. Inhibitory fragment from the p41 form of invariant chain can regulate activity of cysteine cathepsins in antigen presentation. (nih.gov)
Proteins1
  • In our cells, it processes proteins for the immune system, generating the short peptides displayed by MHC , and has been called asparaginyl endopeptidase (based on its preference for cleaving proteins after asparagine). (rcsb.org)
Inhibitors2
  • This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS . (nih.gov)
  • SP-B control in type II pneumocytes can be delicate to treatment with cysteine-cathepsin inhibitors and research demonstrated that Ctsh can be capable of control SP-B [14], [19]. (perlierusa.com)
Peptidases9
  • Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. (embl.de)
  • Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. (embl.de)
  • Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. (embl.de)
  • Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases. (embl.de)
  • 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. (embl.de)
  • Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. (embl.de)
  • Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. (embl.de)
  • Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. (embl.de)
  • The crystal structure of a YkfC ortholog from Bacillus cereus (BcYkfC) at 1.8 Å resolution revealed that it contains two N-terminal bacterial SH3 (SH3b) domains in addition to the C-terminal catalytic NlpC/P60 domain that is ubiquitous in the very large family of cell-wall-related cysteine peptidases. (iucr.org)
Activity1
  • Predicted to act upstream of or within positive regulation of cysteine-type endopeptidase activity and positive regulation of striated muscle cell differentiation. (nih.gov)
Protein5
  • Here we achieved dual control on one residue by genetically encoding S-propargyl-cysteine (SprC), which has bioorthogonal alkyne and propargyl groups in a compact structure, permitting usage in protein interior in addition to surface. (nih.gov)
  • Members of the CCN protein family, including CTGF, are structurally characterized by having four conserved, cysteine -rich domains. (wikipedia.org)
  • These domains are, from N- to C-termini, the insulin-like growth factor binding protein ( IGFBP ) domain, the von Willebrand type C repeats ( vWC ) domain, the thrombospondin type 1 repeat (TSR) domain, and a C-terminal domain (CT) with a cysteine knot motif. (wikipedia.org)
  • Legumain (shown here from PDB entry 4awb ) uses a cysteine amino acid to perform its protein-cutting reaction, assisted by a histidine and an asparagine. (rcsb.org)
  • it replaces the amino acid cysteine with a signal to stop protein production prematurely (written as Cys135Ter or C135X). (medlineplus.gov)
Asparagine3
  • 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. (embl.de)
  • Legumain, with active site cysteine in yellow, histidine and asparagine in orange, and glycosylation in magenta. (rcsb.org)
  • 4. Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice. (nih.gov)
Extracellular1
  • Argingipain, so termed due to its peptide cleavage specificity at arginine residue, is a unique extracellular cysteine proteinase produced by the anaerobic rod Porphyromonas gingivalis, which is known as a major pathogenic factor of the progressive periodontal disease (T, Kadowaki, M. Yoneda, K. Okamoto, K. Maeda, and K, Yamamoto (1994) J. Biol. (elsevier.com)
Molecular1
  • En esas condiciones, una ruta molecular en la que intervienen AMPK y PFKFB3 induce la glucólisis y las células paradas en mitosis muestran unos requerimientos aumentados a la glucosa, una adición que puede tener implicaciones en terapia del cáncer. (sebbm.es)
Amino acid1
  • This ligation reaction occurs in the same active site, but doesn't appear to use the cysteine amino acid. (rcsb.org)
Specificity1
  • CXCR4(D97C) produced little if any covalent complicated with the seven vMIP-II mutants examined (Fig. 1A B). The noticed sensitivity of many biophysical properties from the complicated to specific cysteine positioning suggests specificity from the disulfide-trapping strategy and works with compatibility from the D187C:W5C disulfide connection with the indigenous complicated geometry. (morainetownshipdems.org)
Structurally1
  • Matrix metalloproteinases (MMPs) are a group of structurally related endopeptidases that require a metal cofactor. (medscape.com)
Mutants2
  • Rupatadine We therefore utilized a technique that utilizes disulfide trapping to create an irreversible complicated (13 14 Coexpression of pairs of one cysteine mutants of CXCR4 and vMIP-II was likely to bring about spontaneous formation of the disulfide connection when the disulfide was appropriate for the indigenous geometry from the CKR:chemokine complicated. (morainetownshipdems.org)
  • A) nonreducing SDS-PAGE and Traditional western blot of CXCR4(D97C) (still left) and CXCR4(D187C) (best) coexpressed with cysteine mutants of vMIP-II (residues 1-7). (morainetownshipdems.org)
Acid1
Genes1
  • El uso de modelos animales con mutaciones en genes específicos ha permitido el estudio de la relevancia fisiológica de muchos de esos reguladores en diversos tejidos, así como su potencial terapéutico en modelos de desarrollo tumoral. (sebbm.es)
Group1
  • Plant PCD is effected by a unique group of papain-type cysteine endopeptidases (CysEP) with a C-terminal KDEL endoplasmic reticulum (ER) retention signal (KDEL CysEP). (tum.de)
Complexes1
  • 14) 37 cysteine mutant pairs had been designed and for every set the plethora of disulfide-trapped complexes was examined (15). (morainetownshipdems.org)
Rag1 (recombination activating 1) - Rat Genome Database
Rag1 (recombination activating 1) - Rat Genome Database (rgd.mcw.edu)
Publications | Max Planck Institute of Biochemistry
Publications | Max Planck Institute of Biochemistry (biochem.mpg.de)
MeSH Browser
MeSH Browser (meshb.nlm.nih.gov)
Evaluation of the Efficacy and Safety of ALV003 in Symptomatic in Celiac Disease Patients - Full Text View - ClinicalTrials.gov
Evaluation of the Efficacy and Safety of ALV003 in Symptomatic in Celiac Disease Patients - Full Text View - ClinicalTrials.gov (clinicaltrials.gov)
BIRC7 Protein - Creative BioMart
BIRC7 Protein - Creative BioMart (creativebiomart.net)
KOPS.Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense
KOPS.Endoplasmic reticulum KDEL-tailed cysteine endopeptidase 1 of Arabidopsis (AtCEP1) is involved in pathogen defense (kops.uni-konstanz.de)
2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE: Uses, Interactions, Mechanism of Action |...
2-[(2,4-DICHLORO-5-METHYLPHENYL)SULFONYL]-1,3-DINITRO-5-(TRIFLUOROMETHYL)BENZENE: Uses, Interactions, Mechanism of Action |... (go.drugbank.com)
歯学部門 - 研究成果 - 九州大学
歯学部門 - 研究成果 - 九州大学 (kyushu-u.pure.elsevier.com)
Martin Witte - Research output - the University of Groningen research portal
Martin Witte - Research output - the University of Groningen research portal (research.rug.nl)
Schmid, Markus - Regulation of Plant Growth & Development by the Environment - Umeå Plant Science Centre
Schmid, Markus - Regulation of Plant Growth & Development by the Environment - Umeå Plant Science Centre (upsc.se)
Szl Phenotypes
Szl Phenotypes (xenbase.org)
CIPSM - Research Area B
CIPSM - Research Area B (cipsm.de)
Gingipains from Porphyromonas gingivalis Increase the Chemotactic and Respiratory Burst-Priming Properties of the 77-Amino-Acid...
Gingipains from Porphyromonas gingivalis Increase the Chemotactic and Respiratory Burst-Priming Properties of the 77-Amino-Acid... (research.birmingham.ac.uk)
Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch....
Peptide Mass Fingerprinting and N-Terminal Amino Acid Sequencing of Glycosylated Cysteine Protease of Euphorbia nivulia Buch.... (hindawi.com)
CoP: Co-expressed Biological Processes
CoP: Co-expressed Biological Processes (webs2.kazusa.or.jp)
Bio2Vec
Bio2Vec (bio2vec.cbrc.kaust.edu.sa)
4873 hypothetical proteinThalassiosira pseudonana | Diatom Portal
4873 hypothetical proteinThalassiosira pseudonana | Diatom Portal (networks.systemsbiology.net)
Apoptosis Database
Apoptosis Database (deathbase.org)
Caspase 8 | Profiles RNS
Caspase 8 | Profiles RNS (profiles.rush.edu)
SustainPineDB
SustainPineDB (scbi.uma.es)
InnateDB: Systems Biology of the Innate Immune Response
InnateDB: Systems Biology of the Innate Immune Response (innatedb.com)
Molecular network-based identification of competing endogenous RNAs and mRNA signatures that predict survival in prostate...
Molecular network-based identification of competing endogenous RNAs and mRNA signatures that predict survival in prostate... (translational-medicine.biomedcentral.com)
Expression of SOX7 in cancer - Summary - The Human Protein Atlas
Expression of SOX7 in cancer - Summary - The Human Protein Atlas (v17.proteinatlas.org)